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| | ==Crystal Structure an Tandem Cyanovirin-N Dimer, CVN2L0== | | ==Crystal Structure an Tandem Cyanovirin-N Dimer, CVN2L0== |
| - | <StructureSection load='3s3y' size='340' side='right' caption='[[3s3y]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3s3y' size='340' side='right'caption='[[3s3y]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3s3y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_variabilis_var._ellipsospora Anabaena variabilis var. ellipsospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S3Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S3Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3s3y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S3Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s3z|3s3z]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s3y OCA], [http://pdbe.org/3s3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s3y RCSB], [http://www.ebi.ac.uk/pdbsum/3s3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s3y ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s3y OCA], [https://pdbe.org/3s3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s3y RCSB], [https://www.ebi.ac.uk/pdbsum/3s3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s3y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL]] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref> | + | [https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena variabilis var. ellipsospora]] | + | [[Category: Large Structures]] |
| - | [[Category: Bjorkman, P J]] | + | [[Category: Nostoc ellipsosporum]] |
| - | [[Category: Keeffe, J R]] | + | [[Category: Bjorkman PJ]] |
| - | [[Category: Mayo, S L]] | + | [[Category: Keeffe JR]] |
| - | [[Category: Antiviral protein]] | + | [[Category: Mayo SL]] |
| - | [[Category: Cyanovirin-n]]
| + | |
| - | [[Category: Engineered dimer]]
| + | |
| - | [[Category: Gp120]]
| + | |
| - | [[Category: Sugar-binding]]
| + | |
| Structural highlights
Function
CVN_NOSEL Mannose-binding lectin.[1] [2]
Publication Abstract from PubMed
Cyanovirin-N (CV-N) is a small, cyanobacterial lectin that neutralizes many enveloped viruses, including human immunodeficiency virus type I (HIV-1). This antiviral activity is attributed to two homologous carbohydrate binding sites that specifically bind high mannose glycosylation present on envelope glycoproteins such as HIV-1 gp120. We created obligate CV-N oligomers to determine whether increasing the number of binding sites has an effect on viral neutralization. A tandem repeat of two CV-N molecules (CVN(2)) increased HIV-1 neutralization activity by up to 18-fold compared to wild-type CV-N. In addition, the CVN(2) variants showed extensive cross-clade reactivity and were often more potent than broadly neutralizing anti-HIV antibodies. The improvement in activity and broad cross-strain HIV neutralization exhibited by these molecules holds promise for the future therapeutic utility of these and other engineered CV-N variants.
Designed oligomers of cyanovirin-N show enhanced HIV neutralization.,Keeffe JR, Gnanapragasam PN, Gillespie SK, Yong J, Bjorkman PJ, Mayo SL Proc Natl Acad Sci U S A. 2011 Jul 28. PMID:21799112[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyd MR, Gustafson KR, McMahon JB, Shoemaker RH, O'Keefe BR, Mori T, Gulakowski RJ, Wu L, Rivera MI, Laurencot CM, Currens MJ, Cardellina JH 2nd, Buckheit RW Jr, Nara PL, Pannell LK, Sowder RC 2nd, Henderson LE. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development. Antimicrob Agents Chemother. 1997 Jul;41(7):1521-30. PMID:9210678
- ↑ Botos I, Wlodawer A. Cyanovirin-N: a sugar-binding antiviral protein with a new twist. Cell Mol Life Sci. 2003 Feb;60(2):277-87. PMID:12678493
- ↑ Keeffe JR, Gnanapragasam PN, Gillespie SK, Yong J, Bjorkman PJ, Mayo SL. Designed oligomers of cyanovirin-N show enhanced HIV neutralization. Proc Natl Acad Sci U S A. 2011 Jul 28. PMID:21799112 doi:10.1073/pnas.1108777108
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