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2jmv

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Revision as of 06:39, 25 June 2020

Solution structure of scytovirin refined against residual dipolar couplings

Structural highlights

2jmv is a 1 chain structure with sequence from Scyva. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SVN_SCYVA] Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The solution structure of the potent 95 residue anti-HIV protein scytovirin has been determined and two carbohydrate-binding sites have been identified. This unique protein, containing five structurally important disulfide bonds, demonstrates a novel fold with no elements of extended regular secondary structure. Scytovirin contains two 39 residue sequence repeats, differing in only three amino acid residues, and each repeat has primary sequence similarity to chitin binding proteins. Both sequence repeats form similarly structured domains, with the exception of one region. The result is two carbohydrate-binding sites with substantially different affinities. The unusual fold clusters aromatic residues in both sites, suggesting a binding mechanism similar to other known hevein-like carbohydrate-binding proteins but differing in carbohydrate specificity. Scytovirin, originally isolated from the cyanobacterium Scytonema varium, holds potential as an HIV entry inhibitor for both therapeutic and prophylactic anti-HIV applications. The high-resolution structural studies reported are an important initial step in unlocking the therapeutic potential of scytovirin.

The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors.,McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:17434526^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bokesch HR, O'Keefe BR, McKee TC, Pannell LK, Patterson GM, Gardella RS, Sowder RC 2nd, Turpin J, Watson K, Buckheit RW Jr, Boyd MR. A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. Biochemistry. 2003 Mar 11;42(9):2578-84. doi: 10.1021/bi0205698. PMID:12614152 doi:http://dx.doi.org/10.1021/bi0205698
↑ Xiong C, O'Keefe BR, Byrd RA, McMahon JB. Potent anti-HIV activity of scytovirin domain 1 peptide. Peptides. 2006 Jul;27(7):1668-75. doi: 10.1016/j.peptides.2006.03.018. Epub 2006 , May 2. PMID:16647158 doi:http://dx.doi.org/10.1016/j.peptides.2006.03.018
↑ Ratner DM, Seeberger PH. Carbohydrate microarrays as tools in HIV glycobiology. Curr Pharm Des. 2007;13(2):173-83. doi: 10.2174/138161207779313650. PMID:17269926 doi:http://dx.doi.org/10.2174/138161207779313650
↑ McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA. The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors. J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:17434526 doi:http://dx.doi.org/S0022-2836(07)00371-3
↑ McFeeters RL, Xiong C, O'Keefe BR, Bokesch HR, McMahon JB, Ratner DM, Castelli R, Seeberger PH, Byrd RA. The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors. J Mol Biol. 2007 Jun 1;369(2):451-61. Epub 2007 Mar 20. PMID:17434526 doi:http://dx.doi.org/S0022-2836(07)00371-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jmv"

@@ Line 6: / Line 6: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmv OCA], [http://pdbe.org/2jmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jmv RCSB], [http://www.ebi.ac.uk/pdbsum/2jmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmv ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SVN_SCYVA SVN_SCYVA]] Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin.<ref>PMID:12614152</ref> <ref>PMID:16647158</ref> <ref>PMID:17269926</ref> <ref>PMID:17434526</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2jmv

From Proteopedia

Revision as of 06:39, 25 June 2020

Solution structure of scytovirin refined against residual dipolar couplings

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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