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The crystal structure of human CskSH3: structural diversity near the RT‐Src and n‐Src loop
Author(s) -
Borchert T.V.,
Mathieu M.,
Zeelen J.Ph.,
Courtneidge S.A.,
Wierenga R.K.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80244-0
Subject(s) - sh3 domain , proto oncogene tyrosine protein kinase src , tyrosine kinase , tyrosine , protein structure , kinase , chemistry , biology , biophysics , microbiology and biotechnology , signal transduction , biochemistry
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 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.