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| | ==CYANOVIRIN-N== | | ==CYANOVIRIN-N== |
| - | <StructureSection load='1j4v' size='340' side='right'caption='[[1j4v]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1j4v' size='340' side='right'caption='[[1j4v]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1j4v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_variabilis_var._ellipsospora Anabaena variabilis var. ellipsospora]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1j4v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4V 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;'>[[2ezm|2ezm]], [[2ezn|2ezn]], [[3ezm|3ezm]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4v OCA], [https://pdbe.org/1j4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4v RCSB], [https://www.ebi.ac.uk/pdbsum/1j4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4v 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=1j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4v OCA], [https://pdbe.org/1j4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4v RCSB], [https://www.ebi.ac.uk/pdbsum/1j4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4v 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: Bewley, C A]] | + | [[Category: Nostoc ellipsosporum]] |
| - | [[Category: Clore, G M]] | + | [[Category: Bewley CA]] |
| - | [[Category: Cyanovirin-n]] | + | [[Category: Clore GM]] |
| - | [[Category: Dipolar couplings / conjoined rigid body-torsion angle dynamic]]
| + | |
| - | [[Category: Domain-swapped dimer]]
| + | |
| - | [[Category: Hiv-inactivating]]
| + | |
| - | [[Category: Immune system]]
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| 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
A simple and robust method for determining the relative orientations of covalently linked protein domains using conjoined rigid body/torsion angle dynamics simulated annealing on the basis of residual dipolar couplings is presented. In this approach each domain is treated as a rigid body and the relevant degrees of conformational freedom are restricted to the backbone torsion angles (phi, psi) of the linker between the domains. By this means translational information afforded by the presence of an intact linker is preserved. We illustrate this approach using the domain-swapped dimer of the HIV-inactivating protein cyanovirin-N as an example.
Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings.,Clore GM, Bewley CA J Magn Reson. 2002 Feb;154(2):329-35. PMID:11846592[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
- ↑ Clore GM, Bewley CA. Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings. J Magn Reson. 2002 Feb;154(2):329-35. PMID:11846592 doi:10.1006/jmre.2001.2489
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