2BZY

Homodimer of CrkL-SH3C domain

2BZY の概要

• エントリーDOI: 10.2210/pdb2bzy/pdb
• 関連するPDBエントリー: 2BZX
• 分子名称: CRK-LIKE PROTEIN (1 entity in total)
• 機能のキーワード: crk-like, crkl, sh3 domain, dimer, nuclear export
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15103.23

構造登録者

Harkiolaki, M.,Gilbert, R.J.,Jones, E.Y.,Feller, S.M. (登録日: 2005-08-24, 公開日: 2006-09-28, 最終更新日: 2024-11-20)

主引用文献

Harkiolaki, M.,Gilbert, R.J.,Jones, E.Y.,Feller, S.M.
The C-Terminal SH3 Domain of Crkl as a Dynamic Dimerization Module Transiently Exposing a Nuclear Export Signal.
Structure, 14:1741-, 2006

PubMed Abstract: CRKL plays essential roles in cell signaling. It consists of an N-terminal SH2 domain followed by two SH3 domains. SH2 and SH3N bind to signaling proteins, but the function of the SH3C domain has remained largely enigmatic. We show here that the SH3C of CRKL forms homodimers in protein crystals and in solution. Evidence for dimer formation of full-length CRKL is also presented. In the SH3C dimer, a nuclear export signal (NES) is mostly buried under the domain surface. The same is true for a monomeric SH3C obtained under different crystallization conditions. Interestingly, partial SH3 unfolding, such as occurs upon dimer/monomer transition, produces a fully-accessible NES through translocation of a single beta strand. Our results document the existence of an SH3 domain dimer formed through exchange of the first SH3 domain beta strand and suggest that partial unfolding of the SH3C is important for the relay of information in vivo.

PubMed: 17161365
DOI: 10.1016/J.STR.2006.09.013

実験手法

X-RAY DIFFRACTION (2.5 Å)