2ezm: Difference between revisions
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==SOLUTION NMR STRUCTURE OF CYANOVIRIN-N, RESTRAINED REGULARIZED MEAN COORDINATES== | ==SOLUTION NMR STRUCTURE OF CYANOVIRIN-N, RESTRAINED REGULARIZED MEAN COORDINATES== | ||
<StructureSection load='2ezm' size='340' side='right'caption='[[2ezm | <StructureSection load='2ezm' size='340' side='right'caption='[[2ezm]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ezm]] is a 1 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=2EZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZM FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ezm]] is a 1 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=2EZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZM FirstGlance]. <br> | ||
</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=2ezm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezm OCA], [https://pdbe.org/2ezm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ezm RCSB], [https://www.ebi.ac.uk/pdbsum/2ezm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ezm ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2ezm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezm OCA], [https://pdbe.org/2ezm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ezm RCSB], [https://www.ebi.ac.uk/pdbsum/2ezm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ezm 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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/2ezm_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/2ezm_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Nostoc ellipsosporum]] | [[Category: Nostoc ellipsosporum]] | ||
[[Category: Bewley | [[Category: Bewley CA]] | ||
[[Category: Clore | [[Category: Clore GM]] | ||
[[Category: Gronenborn | [[Category: Gronenborn AM]] | ||
Latest revision as of 08:11, 17 October 2024
SOLUTION NMR STRUCTURE OF CYANOVIRIN-N, RESTRAINED REGULARIZED MEAN COORDINATESSOLUTION NMR STRUCTURE OF CYANOVIRIN-N, RESTRAINED REGULARIZED MEAN COORDINATES
Structural highlights
FunctionCVN_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 PubMedThe solution structure of cyanovirin-N, a potent 11,000 Mr HIV-inactivating protein that binds with high affinity and specificity to the HIV surface envelope protein gp120, has been solved by nuclear magnetic resonance spectroscopy, including extensive use of dipolar couplings which provide a priori long range structural information. Cyanovirin-N is an elongated, largely beta-sheet protein that displays internal two-fold pseudosymmetry. The two sequence repeats (residues 1-50 and 51-101) share 32% sequence identity and superimpose with a backbone atomic root-mean-square difference of 1.3 A. The two repeats, however, do not form separate domains since the overall fold is dependent on numerous contacts between them. Rather, two symmetrically related domains are formed by strand exchange between the two repeats. Analysis of surface hydrophobic clusters suggests the location of potential binding sites for protein-protein interactions. Solution structure of cyanovirin-N, a potent HIV-inactivating protein.,Bewley CA, Gustafson KR, Boyd MR, Covell DG, Bax A, Clore GM, Gronenborn AM Nat Struct Biol. 1998 Jul;5(7):571-8. PMID:9665171[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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