3MTT

Crystal structure of iSH2 domain of human p85beta, Northeast Structural Genomics Consortium Target HR5531C

3MTT の概要

• エントリーDOI: 10.2210/pdb3mtt/pdb
• 分子名称: Phosphatidylinositol 3-kinase regulatory subunit beta (2 entities in total)
• 機能のキーワード: pi3-kinase subunit p85-beta, inter-sh2 domain, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, signaling protein, protein binding
• 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: 22748.60

構造登録者

Guan, R.,Schauder, C.,Ma, L.C.,Krug, R.M.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2010-04-30, 公開日: 2010-05-19, 最終更新日: 2024-11-27)

主引用文献

Schauder, C.,Ma, L.C.,Krug, R.M.,Montelione, G.T.,Guan, R.
Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85beta subunit reveals conformational plasticity in the interhelical turn region
Acta Crystallogr.,Sect.F, 66:1567-1571, 2010

PubMed Abstract: Phosphatidylinositol 3-kinase (PI3K) proteins actively trigger signaling pathways leading to cell growth, proliferation and survival. These proteins have multiple isoforms and consist of a catalytic p110 subunit and a regulatory p85 subunit. The iSH2 domain of the p85β isoform has been implicated in the binding of nonstructural protein 1 (NS1) of influenza A viruses. Here, the crystal structure of human p85β iSH2 determined to 3.3 Å resolution is reported. The structure reveals that this domain mainly consists of a coiled-coil motif. Comparison with the published structure of the bovine p85β iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. By comparing this human p85β iSH2 structure with the bovine p85β iSH2 domain, which shares 99% sequence identity, and by comparing the multiple conformations observed within the asymmetric unit of the bovine iSH2 structure, it was found that this coiled-coil domain exhibits a certain degree of conformational variability or `plasticity' in the interhelical turn region. It is speculated that this plasticity of p85β iSH2 may play a role in regulating its functional and molecular-recognition properties.

PubMed: 21139197
DOI: 10.1107/S1744309110041333

実験手法

X-RAY DIFFRACTION (3.3 Å)