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2BQQ

X-ray Structure of the N-terminal Domain of Human Doublecortin

2BQQ の概要
エントリーDOI10.2210/pdb2bqq/pdb
関連するPDBエントリー1MJD
分子名称NEURONAL MIGRATION PROTEIN DOUBLECORTIN (2 entities in total)
機能のキーワードdcx domain, ubiquitin-like fold, microtubule associated, signaling protein, transferase
由来する生物種HOMO SAPIENS (HUMAN)
タンパク質・核酸の鎖数1
化学式量合計12944.31
構造登録者
Kim, M.H.,Cooper, D.R.,Derewenda, U.,Derewenda, Z.S. (登録日: 2005-04-27, 公開日: 2006-07-19, 最終更新日: 2023-12-13)
主引用文献Cierpicki, T.,Kim, M.H.,Cooper, D.R.,Derewenda, U.,Bushweller, J.H.,Derewenda, Z.S.
The Dc-Module of Doublecortin: Dynamics, Domain Boundaries, and Functional Implications.
Proteins, 64:874-, 2006
Cited by
PubMed Abstract: 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.
PubMed: 16835924
DOI: 10.1002/PROT.21068
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 2bqq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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