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

被引：62

作者：

BORCHERT, TV ^{[1
]}

MATHIEU, M ^{[1
]}

ZEELEN, JP ^{[1
]}

COURTNEIDGE, SA ^{[1
]}

WIERENGA, RK ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,D-69012 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1994年 / 341卷 / 01期

关键词：

FYN; CSK; SRC; CRYSTAL STRUCTURE; AVERAGING; TYROSINE KINASE;

D O I：

10.1016/0014-5793(94)80244-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 Angstrom, 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 Trp(47), 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.

引用

页码：79 / 85

页数：7

共 35 条

[1]

[Anonymous], 1992, X PLOR VERSION 3 1 S

[2] SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85-ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE [J].