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| | <StructureSection load='1lom' size='340' side='right'caption='[[1lom]], [[Resolution|resolution]] 1.72Å' scene=''> | | <StructureSection load='1lom' size='340' side='right'caption='[[1lom]], [[Resolution|resolution]] 1.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lom]] 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=1LOM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LOM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lom]] 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=1LOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ezm|3ezm]], [[1l5b|1l5b]], [[1l5e|1l5e]]</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]], [[1l5b|1l5b]], [[1l5e|1l5e]]</div></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=1lom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lom OCA], [http://pdbe.org/1lom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lom RCSB], [http://www.ebi.ac.uk/pdbsum/1lom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lom 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=1lom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lom OCA], [https://pdbe.org/1lom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lom RCSB], [https://www.ebi.ac.uk/pdbsum/1lom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lom 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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| 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 potent 11 kDa HIV-inactivating protein that binds with high affinity to the HIV surface envelope protein gp120. A double mutant P51S/S52P of CV-N was engineered by swapping two critical hinge-region residues Pro51 and Ser52. This mutant has biochemical and biophysical characteristics equivalent to the wild-type CV-N and its structure resembles that of wild-type CV-N. However, the mutant shows a different orientation in the hinge region that connects two domains of the protein. The observation that this double mutant crystallizes under a wide variety of conditions challenges some of the current hypotheses on domain swapping and on the role of hinge-region proline residues in domain orientation. The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain-swapped CV-N mutants.
Domain-swapped structure of a mutant of cyanovirin-N.,Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761[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
- ↑ Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A. Domain-swapped structure of a mutant of cyanovirin-N. Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761 doi:10.1016/S0006-291X(02)00455-2
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