The crystal structure of human CskSH3: structural diversity near the RT‐Src and n‐Src loop

FEBS Letters

Mathieu, M.¹  Courtneidge, S.A.¹  Wierenga, R.K.¹  Zeelen, J.Ph.¹  Borchert, T.V.¹ 

[1] EMBL, Postfach 102209, D-69012 Heidelberg, Germany

关键词: Fyn;    Csk;    Src;    Crystal structure;    Averaging;    Tyrosine kinase;    DTT;    1;    4-dithiothreitol;    EDTA;    ethylenediaminetetraacetic acid;    TEA;    triethanolamine;   

DOI  :  10.1016/0014-5793(94)80244-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å, with an R-factor of 22.4%. The structure is very similar to the FynSHS crystal structure. When comparing CskSHS 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.

【 授权许可】

Unknown