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3s3y

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Current revision (12:46, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3s3y' size='340' side='right'caption='[[3s3y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3s3y' size='340' side='right'caption='[[3s3y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s3y]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3S3Y FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s3z|3s3z]]</div></td></tr>
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<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'>[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>
<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 ==
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[[https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL]] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref>
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[https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:21799112</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s3y" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anabaena variabilis var. ellipsospora]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bjorkman, P J]]
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[[Category: Nostoc ellipsosporum]]
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[[Category: Keeffe, J R]]
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[[Category: Bjorkman PJ]]
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[[Category: Mayo, S L]]
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[[Category: Keeffe JR]]
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[[Category: Antiviral protein]]
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[[Category: Mayo SL]]
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[[Category: Cyanovirin-n]]
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[[Category: Engineered dimer]]
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[[Category: Gp120]]
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[[Category: Sugar-binding]]
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Current revision

Crystal Structure an Tandem Cyanovirin-N Dimer, CVN2L0

PDB ID 3s3y

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