2LQW

Solution structure of phosphorylated CRKL

2LQW の概要

• エントリーDOI: 10.2210/pdb2lqw/pdb
• NMR情報: BMRB: 18333
• 分子名称: Crk-like protein (1 entity in total)
• 機能のキーワード: sh2, sh3, v-crk sarcoma virus ct10, oncogene homolog, (avian)-like, pcrkl, 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: 33896.89

構造登録者

Jankowski, W.,Saleh, T.,Kalodimos, C. (登録日: 2012-03-16, 公開日: 2012-05-16, 最終更新日: 2024-11-20)

主引用文献

Jankowski, W.,Saleh, T.,Pai, M.T.,Sriram, G.,Birge, R.B.,Kalodimos, C.G.
Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII.
Nat.Chem.Biol., 8:590-596, 2012

PubMed Abstract: CrkL is a key signaling protein that mediates the leukemogenic activity of Bcr-Abl. CrkL is thought to adopt a structure that is similar to that of its CrkII homolog. The two proteins share high sequence identity and indistinguishable ligand binding preferences, yet they have distinct physiological roles. Here we show that the structures of CrkL and phosphorylated CrkL are markedly different than the corresponding structures of CrkII. As a result, the binding activities of the Src homology 2 and Src homology 3 domains in the two proteins are regulated in a distinct manner and to a different extent. The different structural architecture of CrkL and CrkII may account for their distinct functional roles. The data show that CrkL forms a constitutive complex with Abl, thus explaining the strong preference of Bcr-Abl for CrkL. The results also highlight how the structural organization of the modular domains in adaptor proteins can control signaling outcome.

PubMed: 22581121
DOI: 10.1038/nchembio.954

実験手法

SOLUTION NMR