2bqq

From Proteopedia

---

Revision as of 18:59, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 2bqq, resolution 2.200Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known diseases associated with this structure: Lissencephaly, X-linked OMIM:[300121], Subcortical laminal heteropia, X-linked OMIM:[300121]

About this Structure

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

Reference

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 Nov 12 21:05:35 2007