1UUJ

N-terminal domain of Lissencephaly-1 protein (Lis-1)

1UUJ の概要

• エントリーDOI: 10.2210/pdb1uuj/pdb
• 分子名称: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB ALPHA SUBUNIT, SULFATE ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: platelet-activating factor acetylhydrolase, mitosis, neurogenesis, cytoskeleton, cell division, microtubule
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 41654.03

構造登録者

Cooper, D.R.,Kim, M.H.,Devedjiev, Y.,Derewenda, U.,Derewenda, Z.S. (登録日: 2003-12-22, 公開日: 2004-07-29, 最終更新日: 2024-10-23)

主引用文献

Kim, M.H.,Cooper, D.R.,Oleksy, A.,Devedjiev, Y.,Derewenda, U.,Reiner, O.,Otlewski, J.,Derewenda, Z.S.
The Structure of the N-Terminal Domain of the Product of the Lissencephaly Gene Lis1 and its Functional Implications
Structure, 12:987-, 2004

PubMed Abstract: Mutations in the Lis1 gene result in lissencephaly (smooth brain), a debilitating developmental syndrome caused by the impaired ability of postmitotic neurons to migrate to their correct destination in the cerebral cortex. Sequence similarities suggest that the LIS1 protein contains a C-terminal seven-blade beta-propeller domain, while the structure of the N-terminal fragment includes the LisH (Lis-homology) motif, a pattern found in over 100 eukaryotic proteins with a hitherto unknown function. We present the 1.75 A resolution crystal structure of the N-terminal domain of mouse LIS1, and we show that the LisH motif is a novel, thermodynamically very stable dimerization domain. The structure explains the molecular basis of a low severity form of lissencephaly.

PubMed: 15274919
DOI: 10.1016/J.STR.2004.03.024

実験手法

X-RAY DIFFRACTION (1.75 Å)