3I00

Crystal Structure of the huntingtin interacting protein 1 coiled coil domain

3I00 の概要

• エントリーDOI: 10.2210/pdb3i00/pdb
• 分子名称: Huntingtin-interacting protein 1 (2 entities in total)
• 機能のキーワード: transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O00291
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28387.44

構造登録者

Wilbur, J.D.,Hwang, P.K.,Brodsky, F.M.,Fletterick, R.J. (登録日: 2009-06-24, 公開日: 2010-02-23, 最終更新日: 2024-11-06)

主引用文献

Wilbur, J.D.,Hwang, P.K.,Brodsky, F.M.,Fletterick, R.J.
Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain.
Acta Crystallogr.,Sect.D, 66:314-318, 2010

PubMed Abstract: Huntingtin-interacting protein 1 (HIP1) is an important link between the actin cytoskeleton and clathrin-mediated endocytosis machinery. HIP1 has also been implicated in the pathogenesis of Huntington's disease. The binding of HIP1 to actin is regulated through an interaction with clathrin light chain. Clathrin light chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding. To understand the mechanism of this conformational regulation, a high-resolution crystal structure of a stable fragment from the HIP1 coiled-coil domain was determined. The flexibility of the HIP1 coiled-coil region was evident from its variation from a previously determined structure of a similar region. A hydrogen-bond network and changes in coiled-coil monomer interaction suggest that the HIP1 coiled-coil domain is uniquely suited to allow conformational flexibility.

PubMed: 20179344
DOI: 10.1107/S0907444909054535

実験手法

X-RAY DIFFRACTION (2.3 Å)