SVN_SCYVA
ID SVN_SCYVA Reviewed; 95 AA.
AC P86041;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Scytovirin {ECO:0000303|PubMed:12614152};
DE Short=SVN {ECO:0000303|PubMed:16647158};
OS Scytonema varium.
OC Bacteria; Cyanobacteria; Nostocales; Scytonemataceae; Scytonema.
OX NCBI_TaxID=423208;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC STRAIN=HG-24-1 {ECO:0000269|PubMed:12614152};
RX PubMed=12614152; DOI=10.1021/bi0205698;
RA Bokesch H.R., O'Keefe B.R., McKee T.C., Pannell L.K., Patterson G.M.L.,
RA Gardella R.S., Sowder R.C. II, Turpin J., Watson K., Buckheit R.W. Jr.,
RA Boyd M.R.;
RT "A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema
RT varium.";
RL Biochemistry 42:2578-2584(2003).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=16647158; DOI=10.1016/j.peptides.2006.03.018;
RA Xiong C., O'Keefe B.R., Byrd R.A., McMahon J.B.;
RT "Potent anti-HIV activity of scytovirin domain 1 peptide.";
RL Peptides 27:1668-1675(2006).
RN [3] {ECO:0000305}
RP SYNTHESIS.
RX PubMed=16289703; DOI=10.1016/j.pep.2005.09.019;
RA Xiong C., O'Keefe B.R., Botos I., Wlodawer A., McMahon J.B.;
RT "Overexpression and purification of scytovirin, a potent, novel anti-HIV
RT protein from the cultured cyanobacterium Scytonema varium.";
RL Protein Expr. Purif. 46:233-239(2006).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=17269926; DOI=10.2174/138161207779313650;
RA Ratner D.M., Seeberger P.H.;
RT "Carbohydrate microarrays as tools in HIV glycobiology.";
RL Curr. Pharm. Des. 13:173-183(2007).
RN [5] {ECO:0000305}
RP STRUCTURE BY NMR, AND FUNCTION.
RX PubMed=17434526; DOI=10.1016/j.jmb.2007.03.030;
RA McFeeters R.L., Xiong C., O'Keefe B.R., Bokesch H.R., McMahon J.B.,
RA Ratner D.M., Castelli R., Seeberger P.H., Byrd R.A.;
RT "The novel fold of scytovirin reveals a new twist for antiviral entry
RT inhibitors.";
RL J. Mol. Biol. 369:451-461(2007).
RN [6] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=17965185; DOI=10.1110/ps.073157507;
RA Moulaei T., Botos I., Ziolkowska N.E., Bokesch H.R., Krumpe L.R.,
RA McKee T.C., O'Keefe B.R., Dauter Z., Wlodawer A.;
RT "Atomic-resolution crystal structure of the antiviral lectin scytovirin.";
RL Protein Sci. 16:2756-2760(2007).
CC -!- FUNCTION: Has strong anti-HIV activity against T-tropic strains of HIV-
CC 1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1
CC fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits
CC fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and
CC fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells.
CC Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding
CC to HIV gp120 is glycosylation dependent. Binds with high specificity to
CC the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and
CC also binds the higher-order oligosaccharides oligomannose 8 and
CC oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-
CC linked oligosaccharides or chitin. {ECO:0000269|PubMed:12614152,
CC ECO:0000269|PubMed:16647158, ECO:0000269|PubMed:17269926,
CC ECO:0000269|PubMed:17434526}.
CC -!- MASS SPECTROMETRY: Mass=9712.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12614152};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 2JMV; NMR; -; A=1-95.
DR PDB; 2QSK; X-ray; 1.00 A; A=1-95.
DR PDB; 2QT4; X-ray; 1.30 A; A=1-95.
DR PDBsum; 2JMV; -.
DR PDBsum; 2QSK; -.
DR PDBsum; 2QT4; -.
DR AlphaFoldDB; P86041; -.
DR SMR; P86041; -.
DR UniLectin; P86041; -.
DR EvolutionaryTrace; P86041; -.
DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral protein; Direct protein sequencing; Disulfide bond;
KW Lectin.
FT CHAIN 1..95
FT /note="Scytovirin"
FT /id="PRO_0000352757"
FT REGION 3..41
FT /note="SD1"
FT REGION 51..89
FT /note="SD2"
FT DISULFID 7..55
FT /evidence="ECO:0000269|PubMed:12614152,
FT ECO:0000269|PubMed:17965185"
FT DISULFID 20..32
FT /evidence="ECO:0000269|PubMed:17965185"
FT DISULFID 26..38
FT /evidence="ECO:0000269|PubMed:17965185"
FT DISULFID 68..80
FT /evidence="ECO:0000269|PubMed:17965185"
FT DISULFID 74..86
FT /evidence="ECO:0000269|PubMed:17965185"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:2JMV"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2JMV"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2JMV"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2QSK"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2QSK"
SQ SEQUENCE 95 AA; 9722 MW; E8F34DFB2E7659AC CRC64;
GSGPTYCWNE ANNPGGPNRC SNNKQCDGAR TCSSSGFCQG TSRKPDPGPK GPTYCWDEAK
NPGGPNRCSN SKQCDGARTC SSSGFCQGTA GHAAA
