2L3P

Structure of the prolyl cis isomer of the Crk Protein

2L3P の概要

• エントリーDOI: 10.2210/pdb2l3p/pdb
• 関連するPDBエントリー: 2L3Q 2L3S
• 分子名称: Cis isomer of Crk protein (1 entity in total)
• 機能のキーワード: adapter protein, structural protein
• 由来する生物種: Gallus gallus (bantam,chickens)
• 細胞内の位置: Cytoplasm (By similarity): Q04929
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8731.95

構造登録者

Kalodimos, C.G.,Sarkar, P.,Saleh, T.,Tzeng, S.R.,Birge, R. (登録日: 2010-09-21, 公開日: 2010-12-08, 最終更新日: 2024-05-01)

主引用文献

Sarkar, P.,Saleh, T.,Tzeng, S.R.,Birge, R.B.,Kalodimos, C.G.
Structural basis for regulation of the Crk signaling protein by a proline switch.
Nat.Chem.Biol., 7:51-57, 2011

PubMed Abstract: Proline switches, controlled by cis-trans isomerization, have emerged as a particularly effective regulatory mechanism in a wide range of biological processes. Here we report the structures of both the cis and trans conformers of a proline switch in the Crk signaling protein. Proline isomerization toggles Crk between two conformations: an autoinhibitory conformation, stabilized by the intramolecular association of two tandem SH3 domains in the cis form, and an uninhibited, activated conformation promoted by the trans form. In addition to acting as a structural switch, the heterogeneous proline recruits cyclophilin A, which accelerates the interconversion rate between the isomers, thereby regulating the kinetics of Crk activation. The data provide atomic insight into the mechanisms that underpin the functionality of this binary switch and elucidate its remarkable efficiency. The results also reveal new SH3 binding surfaces, highlighting the binding versatility and expanding the noncanonical ligand repertoire of this important signaling domain.

PubMed: 21131971
DOI: 10.1038/nchembio.494

実験手法

SOLUTION NMR