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| | <StructureSection load='3czz' size='340' side='right'caption='[[3czz]], [[Resolution|resolution]] 1.36Å' scene=''> | | <StructureSection load='3czz' size='340' side='right'caption='[[3czz]], [[Resolution|resolution]] 1.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3czz]] is a 2 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=3CZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3czz]] is a 2 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=3CZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l5b|1l5b]], [[2z21|2z21]], [[2ezm|2ezm]]</div></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]] 1.36Å</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=3czz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czz OCA], [https://pdbe.org/3czz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3czz RCSB], [https://www.ebi.ac.uk/pdbsum/3czz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3czz 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=3czz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czz OCA], [https://pdbe.org/3czz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3czz RCSB], [https://www.ebi.ac.uk/pdbsum/3czz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3czz 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: Furey, W]] | + | [[Category: Nostoc ellipsosporum]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Furey W]] |
| - | [[Category: Matei, E]] | + | [[Category: Gronenborn AM]] |
| - | [[Category: Antiviral protein]] | + | [[Category: Matei E]] |
| - | [[Category: Cyanovirin-n]]
| + | |
| - | [[Category: Gp120]]
| + | |
| - | [[Category: Hiv-inactivating]]
| + | |
| - | [[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
The cyanobacterial lectin Cyanovirin-N (CV-N) exhibits antiviral activity against HIV at a low nanomolar concentration by interacting with high-mannose oligosaccharides on the virus surface envelope glycoprotein gp120. Atomic structures of wild-type CV-N revealed a monomer in solution and a domain-swapped dimer in the crystal, with the monomer comprising two independent carbohydrate binding sites that individually bind with micromolar affinity to di- and trimannoses. In the mutant CVN(mutDB), the binding site on domain B was abolished and the protein was found to be completely inactive against HIV. We determined the solution NMR and crystal structures of this variant and characterized its sugar binding properties. In solution and the crystal, CVN(mutDB) is a monomer and no domain-swapping was observed. The protein binds to Man-3 and Man-9 with similar dissociation constants ( approximately 4 muM). This confirms that the nanomolar activity of wild-type CV-N is related to the multisite nature of the protein carbohydrate interaction.
Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping.,Matei E, Furey W, Gronenborn AM Structure. 2008 Aug 6;16(8):1183-94. PMID:18682220[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, Furey W, Gronenborn AM. Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping. Structure. 2008 Aug 6;16(8):1183-94. PMID:18682220 doi:10.1016/j.str.2008.05.011
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