2DVJ

phosphorylated Crk-II

2DVJ の概要

• エントリーDOI: 10.2210/pdb2dvj/pdb
• 関連するPDBエントリー: 2EYV 2EYW 2EYX 2EYY 2EYZ
• 分子名称: V-crk sarcoma virus CT10 oncogene homolog, isoform a (1 entity in total)
• 機能のキーワード: sh3, sh2, signal transduction, adapter molecule, signaling protein
• 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: 25525.07

構造登録者

Kobashigawa, Y.,Inagaki, F. (登録日: 2006-07-31, 公開日: 2007-05-08, 最終更新日: 2024-11-20)

主引用文献

Kobashigawa, Y.,Sakai, M.,Naito, M.,Yokochi, M.,Kumeta, H.,Makino, Y.,Ogura, K.,Tanaka, S.,Inagaki, F.
Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK.
Nat.Struct.Mol.Biol., 14:503-510, 2007

PubMed Abstract: CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK that regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. CRKI shows substantial transforming activity, whereas the activity of CRKII is low, and phosphorylated CRKII has no biological activity whatsoever. The molecular mechanisms underlying the distinct biological activities of the CRK proteins remain elusive. We determined the solution structures of CRKI, CRKII and phosphorylated CRKII by NMR and identified the molecular mechanism that gives rise to their activities. Results from mutational analysis using rodent 3Y1 fibroblasts were consistent with those from the structural studies. Together, these data suggest that the linker region modulates the binding of CRKII to its targets, thus regulating cell growth and motility.

PubMed: 17515907
DOI: 10.1038/nsmb1241

実験手法

SOLUTION NMR