1CSK

THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP

1CSK の概要

• エントリーDOI: 10.2210/pdb1csk/pdb
• 分子名称: C-SRC SH3 DOMAIN (2 entities in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): P41240
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 31407.78

構造登録者

Mathieu, M.,Wierenga, R.K. (登録日: 1994-03-22, 公開日: 1994-07-31, 最終更新日: 2024-02-07)

主引用文献

Borchert, T.V.,Mathieu, M.,Zeelen, J.P.,Courtneidge, S.A.,Wierenga, R.K.
The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop.
FEBS Lett., 341:79-85, 1994

PubMed Abstract: SH3 domains are modules occurring in diverse proteins, ranging from cytoskeletal proteins to signaling proteins, such as tyrosine kinases. The crystal structure of the SH3 domain of Csk (c-Src specific tyrosine kinase) has been refined at a resolution of 2.5 A, with an R-factor of 22.4%. The structure is very similar to the FynSH3 crystal structure. When comparing CskSH3 and FynSH3 it is seen that the structural and charge differences of the RT-Src loop and the n-Src loop, near the conserved Trp47, correlate with different binding properties of these SH3 domains. The structure comparison suggests that those glycines and acid residues which are very well conserved in the SH3 sequences are important for the stability of the SH3 fold.

PubMed: 7511113
DOI: 10.1016/0014-5793(94)80244-0

実験手法

X-RAY DIFFRACTION (2.5 Å)