2bqq: Difference between revisions
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<StructureSection load='2bqq' size='340' side='right'caption='[[2bqq]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2bqq' size='340' side='right'caption='[[2bqq]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bqq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2bqq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BQQ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mjd|1mjd]]</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;'>[[1mjd|1mjd]]</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=2bqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bqq OCA], [https://pdbe.org/2bqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bqq RCSB], [https://www.ebi.ac.uk/pdbsum/2bqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bqq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 13:31, 17 February 2021
X-ray Structure of the N-terminal Domain of Human DoublecortinX-ray Structure of the N-terminal Domain of Human Doublecortin
Structural highlights
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 doublecortin-like (DC) domains, which usually occur in tandem, constitute novel microtubule-binding modules. They were first identified in doublecortin (DCX), a protein expressed in migrating neurons, and in the doublecortin-like kinase (DCLK). They are also found in other proteins, including the RP1 gene product which-when mutated-causes a form of inherited blindness. We previously reported an X-ray structure of the N-terminal DC domain of DCLK (N-DCLK), and a solution structure of an analogous module of human doublecortin (N-DCX). These studies showed that the DC domain has a tertiary fold closely reminiscent of ubiquitin and similar to several GTPase-binding domains. We now report an X-ray structure of a mutant of N-DCX, in which the C-terminal fragment (residues 139-147) unexpectedly shows an altered, "open" conformation. However, heteronuclear NMR data show that this C-terminal fragment is only transiently open in solution, and assumes a predominantly "closed" conformation. While the "open" conformation may be artificially stabilized by crystal packing interactions, the observed switching between the "open" and "closed" conformations, which shortens the linker between the two DC-domains by approximately 20 A, is likely to be of functional importance in the control of tubulin polymerization and microtubule bundling by doublecortin. The DC-module of doublecortin: dynamics, domain boundaries, and functional implications.,Cierpicki T, Kim MH, Cooper DR, Derewenda U, Bushweller JH, Derewenda ZS Proteins. 2006 Sep 1;64(4):874-82. PMID:16835924[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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