2bqq: Difference between revisions

Revision as of 02:17, 28 July 2008

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File:2bqq.png

Template:STRUCTURE 2bqq

X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTINX-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN

Template:ABSTRACT PUBMED 16835924

About this StructureAbout this Structure

2BQQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 02:17:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN'''
+===X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN===
-==Overview==
+<!--
-The 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 line below this paragraph, {{ABSTRACT_PUBMED_16835924}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16835924 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16835924}}
 ==About this Structure==
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 [[Category: Transferase]]
 [[Category: Ubiquitin-like fold]]
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