1MRY

crystal structure of an inactive akt2 kinase domain

1MRY の概要

• エントリーDOI: 10.2210/pdb1mry/pdb
• 関連するPDBエントリー: 1MRV
• 分子名称: RAC-beta serine/threonine kinase (2 entities in total)
• 機能のキーワード: agc serine threonine kinase, akt pkb kinase domain, tumorigenesis, x-ray crystal structure, signal transduction, 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: 39313.01

構造登録者

Huang, X.,Begley, M.,Morgenstern, K.A.,Gu, Y.,Rose, P.,Zhao, H.,Zhu, X. (登録日: 2002-09-18, 公開日: 2003-09-23, 最終更新日: 2024-04-03)

主引用文献

Huang, X.,Begley, M.,Morgenstern, K.A.,Gu, Y.,Rose, P.,Zhao, H.,Zhu, X.
Crystal structure of an inactive akt2 kinase domain
Structure, 11:21-30, 2003

PubMed Abstract: Akt/PKB represents a subfamily of three isoforms from the AGC serine/threonine kinase family. Amplification of Akt activity has been implicated in diseases that involve inappropriate cell survival, including a number of human malignancies. The structure of an inactive and unliganded Akt2 kinase domain reveals several features that distinguish it from other kinases. Most of the alpha helix C is disordered. The activation loop in this structure adopts a conformation that appears to sterically hinder the binding of both ATP and peptide substrate. In addition, an intramolecular disulfide bond is observed between two cysteines in the activation loop. Residues within the linker region between the N- and C-terminal lobes also contribute to the inactive conformation by partially occupying the ATP binding site.

PubMed: 12517337
DOI: 10.1016/S0969-2126(02)00937-1

実験手法

X-RAY DIFFRACTION (2.8 Å)