2kox: Difference between revisions
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==NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin== | ==NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin== | ||
<StructureSection load='2kox' size='340' side='right' caption='[[2kox]], [[NMR_Ensembles_of_Models | 640 NMR models]]' scene=''> | <StructureSection load='2kox' size='340' side='right' caption='[[2kox]], [[NMR_Ensembles_of_Models | 640 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[2kox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KOX FirstGlance]. <br> | <table><tr><td colspan='2'>[[2kox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KOX FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k39|2k39]], [[1d3z|1d3z]], [[2nr2|2nr2]], [[1ubq|1ubq]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k39|2k39]], [[1d3z|1d3z]], [[2nr2|2nr2]], [[1ubq|1ubq]]</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=2kox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kox OCA], [http://pdbe.org/2kox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kox RCSB], [http://www.ebi.ac.uk/pdbsum/2kox PDBsum]</span></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=2kox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kox OCA], [http://pdbe.org/2kox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kox RCSB], [http://www.ebi.ac.uk/pdbsum/2kox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kox ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
Revision as of 11:00, 25 July 2018
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMedLong-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four beta-strands separated by up to 15 A in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network. Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition.,Fenwick RB, Esteban-Martin S, Richter B, Lee D, Walter KF, Milovanovic D, Becker S, Lakomek NA, Griesinger C, Salvatella X J Am Chem Soc. 2011 Jul 13;133(27):10336-10339. Epub 2011 Jun 20. PMID:21634390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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