3L21_NAJKA
ID 3L21_NAJKA Reviewed; 71 AA.
AC P01391;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Alpha-cobratoxin {ECO:0000303|PubMed:1317211, ECO:0000303|PubMed:1939183, ECO:0000303|PubMed:2086254, ECO:0000303|PubMed:2279844, ECO:0000303|PubMed:6553056, ECO:0000303|PubMed:6771288, ECO:0000303|PubMed:6930640};
DE Short=Alpha-CT {ECO:0000303|PubMed:18381281, ECO:0000303|PubMed:22223648};
DE Short=Alpha-CbT {ECO:0000303|PubMed:9840221};
DE Short=Alpha-Cbtx {ECO:0000303|PubMed:10574958, ECO:0000303|PubMed:10852927, ECO:0000303|PubMed:11867717, ECO:0000303|PubMed:12133834, ECO:0000303|PubMed:15791209, ECO:0000303|PubMed:9305882};
DE Short=Alpha-Ctx {ECO:0000305};
DE AltName: Full=Alpha-elapitoxin-Nk2a {ECO:0000305};
DE Short=Alpha-EPTX-Nk2a {ECO:0000305};
DE AltName: Full=Long neurotoxin 1;
DE AltName: Full=Siamensis 3 {ECO:0000303|Ref.1};
OS Naja kaouthia (Monocled cobra) (Naja siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8649;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Karlsson E.;
RT "Chemistry of some potent animal toxins.";
RL Experientia 29:1319-1327(1973).
RN [2]
RP PROTEIN SEQUENCE OF 1-17; 24-33 AND 36-68, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=18381281; DOI=10.1074/jbc.m802085200;
RA Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G., Vorontsova O.V.,
RA Ziganshin R.K., Andreeva T.V., Serebryakova M.V., Benoit A., Hogg R.C.,
RA Bertrand D., Tsetlin V.I., Utkin Y.N.;
RT "Naturally occurring disulfide-bound dimers of three-fingered toxins: a
RT paradigm for biological activity diversification.";
RL J. Biol. Chem. 283:14571-14580(2008).
RN [3]
RP FUNCTION.
RX PubMed=6771288; DOI=10.1016/s0021-9258(20)79707-3;
RA Kang S., Maelicke A.;
RT "Fluorescein isothiocyanate-labeled alpha-cobratoxin. Biochemical
RT characterization and interaction with acetylcholine receptor from
RT Electrophorus electricus.";
RL J. Biol. Chem. 255:7326-7332(1980).
RN [4]
RP FUNCTION.
RX PubMed=6553056; DOI=10.1016/s0021-9258(18)32115-x;
RA Martin B.M., Chibber B.A., Maelicke A.;
RT "The sites of neurotoxicity in alpha-cobratoxin.";
RL J. Biol. Chem. 258:8714-8722(1983).
RN [5]
RP FUNCTION.
RX PubMed=2086254; DOI=10.1016/0014-2999(90)94190-9;
RA Alkondon M., Albuquerque E.X.;
RT "Alpha-cobratoxin blocks the nicotinic acetylcholine receptor in rat
RT hippocampal neurons.";
RL Eur. J. Pharmacol. 191:505-506(1990).
RN [6]
RP FUNCTION.
RX PubMed=9053737; DOI=10.1007/bf00171324;
RA Apel C., Ricny J., Wagner G., Wessler I.;
RT "Alpha-bungarotoxin, kappa-bungarotoxin, alpha-cobratoxin and erabutoxin-b
RT do not affect [3H]acetylcholine release from the rat isolated left
RT hemidiaphragm.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 352:646-652(1995).
RN [7]
RP FUNCTION.
RX PubMed=9305882; DOI=10.1074/jbc.272.39.24279;
RA Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P.,
RA Bertrand D., Menez A.;
RT "Only snake curaremimetic toxins with a fifth disulfide bond have high
RT affinity for the neuronal alpha7 nicotinic receptor.";
RL J. Biol. Chem. 272:24279-24286(1997).
RN [8]
RP FUNCTION.
RX PubMed=9840221; DOI=10.1016/s0197-0186(98)00033-3;
RA Dajas-Bailador F., Costa G., Dajas F., Emmett S.;
RT "Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and
RT fasciculin on the nicotine-evoked release of dopamine in the rat striatum
RT in vivo.";
RL Neurochem. Int. 33:307-312(1998).
RN [9]
RP FUNCTION, SYNTHESIS, MUTAGENESIS OF LYS-23; TRP-25; ASP-27; PHE-29; ARG-33;
RP ARG-36; LYS-49 AND PHE-65, AND SITES LYS-23; TRP-25; ASP-27; PHE-29;
RP ARG-33; ARG-36; LYS-49 AND PHE-65.
RX PubMed=10574958; DOI=10.1074/jbc.274.49.34851;
RA Antil S., Servent D., Menez A.;
RT "Variability among the sites by which curaremimetic toxins bind to torpedo
RT acetylcholine receptor, as revealed by identification of the functional
RT residues of alpha-cobratoxin.";
RL J. Biol. Chem. 274:34851-34858(1999).
RN [10]
RP MUTAGENESIS OF TRP-25; ASP-27; ALA-28; PHE-29; ARG-33; LYS-35; ARG-36 AND
RP PHE-65, AND SITES TRP-25; ASP-27; ALA-28; PHE-29; ARG-33; LYS-35; ARG-36
RP AND PHE-65.
RX PubMed=10852927; DOI=10.1074/jbc.m909746199;
RA Antil-Delbeke S., Gaillard C., Tamiya T., Corringer P.-J., Changeux J.-P.,
RA Servent D., Menez A.;
RT "Molecular determinants by which a long chain toxin from snake venom
RT interacts with the neuronal alpha 7-nicotinic acetylcholine receptor.";
RL J. Biol. Chem. 275:29594-29601(2000).
RN [11]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=26221036; DOI=10.1074/jbc.m115.648824;
RA Kudryavtsev D.S., Shelukhina I.V., Son L.V., Ojomoko L.O., Kryukova E.V.,
RA Lyukmanova E.N., Zhmak M.N., Dolgikh D.A., Ivanov I.A., Kasheverov I.E.,
RA Starkov V.G., Ramerstorfer J., Sieghart W., Tsetlin V.I., Utkin Y.N.;
RT "Neurotoxins from snake venoms and alpha-conotoxin ImI inhibit functionally
RT active ionotropic gamma-aminobutyric acid (GABA) receptors.";
RL J. Biol. Chem. 290:22747-22758(2015).
RN [12]
RP FUNCTION ON ALPHA-7/CHRNA7 NACHR, AND SYNTHESIS.
RX PubMed=30025921; DOI=10.1016/j.neuropharm.2018.07.019;
RA Yu J., Zhu X., Zhang L., Kudryavtsev D., Kasheverov I., Lei Y.,
RA Zhangsun D., Tsetlin V., Luo S.;
RT "Species specificity of rat and human alpha7 nicotinic acetylcholine
RT receptors towards different classes of peptide and protein antagonists.";
RL Neuropharmacology 139:226-237(2018).
RN [13]
RP 3D-STRUCTURE MODELING.
RX PubMed=11867717; DOI=10.1073/pnas.042699899;
RA Fruchart-Gaillard C., Gilquin B., Antil-Delbeke S., Le Novere N.,
RA Tamiya T., Corringer P.-J., Changeux J.-P., Menez A., Servent D.;
RT "Experimentally based model of a complex between a snake toxin and the
RT alpha 7 nicotinic receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3216-3221(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=6930640; DOI=10.1073/pnas.77.5.2400;
RA Walkinshaw M.D., Saenger W., Maelicke A.;
RT "Three-dimensional structure of the 'long' neurotoxin from cobra venom.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2400-2404(1980).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=1939183; DOI=10.2210/pdb2ctx/pdb;
RA Betzel C., Lange G., Pal G.P., Wilson K.S., Maelicke A., Saenger W.;
RT "The refined crystal structure of alpha-cobratoxin from Naja naja siamensis
RT at 2.4-A resolution.";
RL J. Biol. Chem. 266:21530-21536(1991).
RN [16]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=2279844; DOI=10.1111/j.1399-3011.1990.tb00971.x;
RA Laplante S.R., Mikou A., Robin M., Guittet E., Delsuc M.-A.,
RA Charpentier I., Lallemand J.-Y.;
RT "Rapid determination and NMR assignments of antiparallel sheets and helices
RT of a scorpion and a cobra toxin.";
RL Int. J. Pept. Protein Res. 36:227-230(1990).
RN [17]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=1317211; DOI=10.1021/bi00135a018;
RA le Goas R., Laplante S.R., Mikou A., Delsuc M.-A., Guittet E., Robin M.,
RA Charpentier I., Lallemand J.-Y.;
RT "Alpha-cobratoxin: proton NMR assignments and solution structure.";
RL Biochemistry 31:4867-4875(1992).
RN [18]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=12133834; DOI=10.1074/jbc.m205483200;
RA Zeng H., Hawrot E.;
RT "NMR-based binding screen and structural analysis of the complex formed
RT between alpha-cobratoxin and an 18-mer cognate peptide derived from the
RT alpha-1 subunit of the nicotinic acetylcholine receptor from Torpedo
RT californica.";
RL J. Biol. Chem. 277:37439-37445(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=15791209; DOI=10.1038/sj.emboj.7600620;
RA Bourne Y., Talley T.T., Hansen S.B., Taylor P., Marchot P.;
RT "Crystal structure of a Cbtx-AChBP complex reveals essential interactions
RT between snake alpha-neurotoxins and nicotinic receptors.";
RL EMBO J. 24:1512-1522(2005).
RN [20]
RP ERRATUM OF PUBMED:15791209.
RA Bourne Y., Talley T.T., Hansen S.B., Taylor P., Marchot P.;
RL EMBO J. 25:266-266(2006).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER),
RP FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=22223648; DOI=10.1074/jbc.m111.322313;
RA Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G.,
RA Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.;
RT "Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular
RT disulfides and possible mode of binding to nicotinic acetylcholine
RT receptors.";
RL J. Biol. Chem. 287:6725-6734(2012).
CC -!- FUNCTION: Monomer: binds with high affinity to muscular (alpha-1-beta-
CC 1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) nAChR (tested on Torpedo
CC californica, Kd=0.2-4.5 nM) and neuronal alpha-7/CHRNA7 nicotinic
CC acetylcholine receptors (Kd=13-105 nM) (PubMed:18381281,
CC PubMed:9305882, PubMed:22223648). Also inhibits GABA(A) channels
CC (PubMed:26221036). Heteropentamer targets studied are composed of
CC alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits (IC(50)=236 nM),
CC alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits (IC(50)=469 nM),
CC alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits (IC(50)=485 nM),
CC alpha-5-beta-3-gamma-2 (GABRA5-GABRB3-GABRG2) subunits (IC(50)=635 nM),
CC and alpha-2-beta-3-gamma-2 (GABRA2-GABRB3-GABRG2) subunits (IC(50)=1099
CC nM) (activated by 10 uM GABA) (PubMed:26221036).
CC {ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:22223648,
CC ECO:0000269|PubMed:26221036, ECO:0000269|PubMed:30025921}.
CC -!- FUNCTION: Homodimer: binds with high affinity (but lower than the
CC monomeric form) to muscular (IC(50)=9.7 nM) and with low affinity to
CC neuronal alpha-7/CHRNA7 nAChRs (IC(50)=1370 nM) (PubMed:22223648).
CC However, it acquires (compared to the monomeric form) the capacity to
CC block alpha-3/beta-2 (CHRNA3/CHRNB2) nAChRs (PubMed:18381281).
CC {ECO:0000269|PubMed:18381281, ECO:0000269|PubMed:22223648}.
CC -!- FUNCTION: Heterodimer with cytotoxin 3 (AC P01446): is slightly more
CC active than the homodimer in inhibiting alpha-7/CHRNA7 nAChR and is
CC considerably more active in blocking the alpha-3-beta-2/CHRNA3-CHRNB2
CC nAChR. {ECO:0000269|PubMed:22223648}.
CC -!- SUBUNIT: Monomer, homo- or heterodimer with cytotoxins 1 (P60305), 2
CC (AC P01445), and 3 (AC P01446); disulfide-linked.
CC {ECO:0000269|PubMed:12133834, ECO:0000269|PubMed:1317211,
CC ECO:0000269|PubMed:15791209, ECO:0000269|PubMed:18381281,
CC ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
CC ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- PTM: In homodimer alpha-cobratoxin, selective reduction of Cys(26)-
CC Cys(30) in one subunit does not affect the activity against the alpha-
CC 7/CHRNA7 nAChR, whereas its reduction in both subunits almost prevents
CC alpha-7/CHRNA7 nAChR recognition. On the contrary, reduction of one or
CC both Cys(26)-Cys(30) disulfide bonds in the homodimer considerably
CC potentiates inhibition of the alpha-3-beta-2/CHRNA3-CHRNB2 nAChR by the
CC toxin. {ECO:0000269|PubMed:22223648}.
CC -!- MISCELLANEOUS: The monomeric form has no effect on alpha-3/beta-2
CC (CHRNA3/CHRNB2) nAChR (PubMed:18381281). It does not show any blockade
CC of the nicotine-evoked release of dopamine (PubMed:9840221) and does
CC not affect ACh release. {ECO:0000269|PubMed:18381281,
CC ECO:0000269|PubMed:9840221}.
CC -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC 6-Thr-Pro-7 (Probable). In the dimeric form, the Pro-7 is extended away
CC from the toxin core whereas in the monomeric form, Pro-7 makes a turn
CC (PubMed:22223648). {ECO:0000269|PubMed:22223648, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR PIR; A01662; N2NJ1S.
DR PDB; 1CTX; X-ray; 2.80 A; A=1-71.
DR PDB; 1LXG; NMR; -; A=1-71.
DR PDB; 1LXH; NMR; -; A=1-71.
DR PDB; 1YI5; X-ray; 4.20 A; F/G/H/I/J=1-71.
DR PDB; 4AEA; X-ray; 1.94 A; A/B=1-71.
DR PDB; 6ZFM; X-ray; 1.90 A; A/B/D/E=1-71.
DR PDB; 7PC0; EM; 3.00 A; K/L=1-71.
DR PDBsum; 1CTX; -.
DR PDBsum; 1LXG; -.
DR PDBsum; 1LXH; -.
DR PDBsum; 1YI5; -.
DR PDBsum; 4AEA; -.
DR PDBsum; 6ZFM; -.
DR PDBsum; 7PC0; -.
DR AlphaFoldDB; P01391; -.
DR SMR; P01391; -.
DR BindingDB; P01391; -.
DR ChEMBL; CHEMBL4739673; -.
DR EvolutionaryTrace; P01391; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..71
FT /note="Alpha-cobratoxin"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000093554"
FT SITE 23
FT /note="Binds to Torpedo AChR"
FT /evidence="ECO:0000269|PubMed:10574958"
FT SITE 25
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT SITE 27
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT SITE 28
FT /note="Binds to alpha-7/CHRNA7 AChR"
FT /evidence="ECO:0000269|PubMed:10852927"
FT SITE 29
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT SITE 33
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT SITE 35
FT /note="Binds to alpha-7/CHRNA7 AChR"
FT /evidence="ECO:0000269|PubMed:10852927"
FT SITE 36
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs, may be important for inhibition of GABA(A)
FT receptors"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927, ECO:0000305|PubMed:26221036"
FT SITE 49
FT /note="Binds to Torpedo AChR"
FT /evidence="ECO:0000269|PubMed:10574958"
FT SITE 65
FT /note="Binds to both neuronal alpha-7/CHRNA7 and Torpedo
FT AChRs"
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT DISULFID 3..20
FT /note="In monomer, partial"
FT /evidence="ECO:0000269|PubMed:12133834,
FT ECO:0000269|PubMed:1317211, ECO:0000269|PubMed:15791209,
FT ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:2279844,
FT ECO:0000269|PubMed:6930640, ECO:0007744|PDB:1CTX,
FT ECO:0007744|PDB:1LXG, ECO:0007744|PDB:1LXH,
FT ECO:0007744|PDB:1YI5"
FT DISULFID 3
FT /note="Interchain (with C-20); in homodimer; partial"
FT /evidence="ECO:0000269|PubMed:22223648,
FT ECO:0007744|PDB:4AEA"
FT DISULFID 14..41
FT /evidence="ECO:0000269|PubMed:12133834,
FT ECO:0000269|PubMed:1317211, ECO:0000269|PubMed:15791209,
FT ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
FT ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640,
FT ECO:0007744|PDB:1CTX, ECO:0007744|PDB:1LXG,
FT ECO:0007744|PDB:1LXH, ECO:0007744|PDB:1YI5,
FT ECO:0007744|PDB:4AEA"
FT DISULFID 20
FT /note="Interchain (with C-3); in homodimer; partial"
FT /evidence="ECO:0000269|PubMed:22223648,
FT ECO:0007744|PDB:4AEA"
FT DISULFID 26..30
FT /evidence="ECO:0000269|PubMed:12133834,
FT ECO:0000269|PubMed:1317211, ECO:0000269|PubMed:15791209,
FT ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
FT ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640,
FT ECO:0007744|PDB:1CTX, ECO:0007744|PDB:1LXG,
FT ECO:0007744|PDB:1LXH, ECO:0007744|PDB:1YI5,
FT ECO:0007744|PDB:4AEA"
FT DISULFID 45..56
FT /evidence="ECO:0000269|PubMed:12133834,
FT ECO:0000269|PubMed:1317211, ECO:0000269|PubMed:15791209,
FT ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
FT ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640,
FT ECO:0007744|PDB:1CTX, ECO:0007744|PDB:1LXG,
FT ECO:0007744|PDB:1LXH, ECO:0007744|PDB:1YI5,
FT ECO:0007744|PDB:4AEA"
FT DISULFID 57..62
FT /evidence="ECO:0000269|PubMed:12133834,
FT ECO:0000269|PubMed:1317211, ECO:0000269|PubMed:15791209,
FT ECO:0000269|PubMed:1939183, ECO:0000269|PubMed:22223648,
FT ECO:0000269|PubMed:2279844, ECO:0000269|PubMed:6930640,
FT ECO:0007744|PDB:1CTX, ECO:0007744|PDB:1LXG,
FT ECO:0007744|PDB:1LXH, ECO:0007744|PDB:1YI5,
FT ECO:0007744|PDB:4AEA"
FT MUTAGEN 23
FT /note="K->E: 2-fold and 28-fold decrease in affinity for
FT Torpedo AChRs."
FT /evidence="ECO:0000269|PubMed:10574958"
FT MUTAGEN 25
FT /note="W->A: 11-fold decrease in affinity for Torpedo AChRs
FT and 6-fold decrease in affinity for neuronal alpha-7/CHRNA7
FT AChR."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT MUTAGEN 27
FT /note="D->R: 31-fold decrease in affinity for Torpedo AChRs
FT and 50-fold decrease in affinity for neuronal alpha-
FT 7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT MUTAGEN 28
FT /note="A->G: 5-fold decrease in affinity for neuronal
FT alpha-7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10852927"
FT MUTAGEN 29
FT /note="F->A: 12-fold decrease in affinity for Torpedo AChRs
FT and 74-fold decrease in affinity for neuronal alpha-
FT 7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT MUTAGEN 33
FT /note="R->E: 767-fold decrease in affinity for Torpedo
FT AChRs and 339-fold decrease in affinity for neuronal alpha-
FT 7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT MUTAGEN 35
FT /note="K->A: 11-fold decrease in affinity for neuronal
FT alpha-7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10852927"
FT MUTAGEN 36
FT /note="R->A: 16-fold decrease in affinity for Torpedo
FT AChRs."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT MUTAGEN 49
FT /note="K->E: 3-fold and 53-fold decrease in affinity for
FT Torpedo AChRs."
FT /evidence="ECO:0000269|PubMed:10574958"
FT MUTAGEN 65
FT /note="F->A: 7-fold decrease in affinity for Torpedo AChRs
FT and 15-fold decrease in affinity for neuronal alpha-
FT 7/CHRNA7 AChR."
FT /evidence="ECO:0000269|PubMed:10574958,
FT ECO:0000269|PubMed:10852927"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6ZFM"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6ZFM"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6ZFM"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1LXG"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6ZFM"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6ZFM"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6ZFM"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1LXG"
SQ SEQUENCE 71 AA; 7831 MW; 6F07ADD885E9AC33 CRC64;
IRCFITPDIT SKDCPNGHVC YTKTWCDAFC SIRGKRVDLG CAATCPTVKT GVDIQCCSTD
NCNPFPTRKR P
