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| | <StructureSection load='3lhc' size='340' side='right'caption='[[3lhc]], [[Resolution|resolution]] 1.34Å' scene=''> | | <StructureSection load='3lhc' size='340' side='right'caption='[[3lhc]], [[Resolution|resolution]] 1.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lhc]] 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=3LHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LHC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lhc]] 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=3LHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LHC FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.34Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ezm|3ezm]], [[1lom|1lom]], [[2ezm|2ezm]]</div></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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3lhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lhc OCA], [https://pdbe.org/3lhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lhc RCSB], [https://www.ebi.ac.uk/pdbsum/3lhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lhc 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=3lhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lhc OCA], [https://pdbe.org/3lhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lhc RCSB], [https://www.ebi.ac.uk/pdbsum/3lhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lhc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena variabilis var. ellipsospora]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aiken, C]] | + | [[Category: Nostoc ellipsosporum]] |
| - | [[Category: Furey, W]] | + | [[Category: Aiken C]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Furey W]] |
| - | [[Category: Matei, E]] | + | [[Category: Gronenborn AM]] |
| - | [[Category: Rose, J]] | + | [[Category: Matei E]] |
| - | [[Category: Zheng, A]] | + | [[Category: Rose J]] |
| - | [[Category: Antiviral protein]]
| + | [[Category: Zheng A]] |
| - | [[Category: Cyanovirin-n]]
| + | |
| - | [[Category: Gp120]]
| + | |
| - | [[Category: Hiv-inactivating]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Protein synthesis inhibitor]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
CVN_NOSEL Mannose-binding lectin.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cyanovirin-N (CV-N) is a two-domain, cyanobacterial protein that inhibits human immunodeficiency virus (HIV) at nanomolar concentrations by binding to high mannose sugars on the HIV envelope glycoprotein gp120. The wild type protein can exist as a monomer or a domain-swapped dimer with the monomer and dimer containing two or four sugar binding sites, respectively, one on each domain. Here we demonstrate that monomeric, single binding site mutants are completely inactive and that a single site, whether located on domain A or B, is insufficient to impart the antiviral activity. Linking inactive, monomeric proteins in a head-to-head fashion by an intermolecular disulfide bond or by creating an exclusively domain-swapped dimer via a hinge residue deletion restored antiviral activity to levels similar to that of wild type CV-N. These findings demonstrate unequivocally that multisite binding by CV-N type lectins is necessary for viral inhibition.
Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization.,Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM J Biol Chem. 2010 Apr 23;285(17):13057-65. Epub 2010 Feb 10. PMID:20147291[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
- ↑ Matei E, Zheng A, Furey W, Rose J, Aiken C, Gronenborn AM. Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization. J Biol Chem. 2010 Apr 23;285(17):13057-65. Epub 2010 Feb 10. PMID:20147291 doi:10.1074/jbc.M109.094938
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