1j4v: Difference between revisions
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<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]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j4v]] is a 2 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ezm|2ezm]], [[2ezn|2ezn]], [[3ezm|3ezm]]</td></tr> | </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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:16, 14 April 2021
CYANOVIRIN-NCYANOVIRIN-N
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 PubMedA 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
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