Open AccessStructure and dynamic regulation of Src-family kinases
Author(s) -
John R. Engen,
Thomas E. Wales,
James Michael Hochrein,
Malcolm A. Meyn,
S. Banu Ozkan,
İvet Bahar,
Thomas E. Smithgall
Publication year - 2008
Publication title -
cellular and molecular life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.928
H-Index - 223
eISSN - 1420-9071
pISSN - 1420-682X
DOI - 10.1007/s00018-008-8122-2
Subject(s) - proto oncogene tyrosine protein kinase src , sh3 domain , tyrosine protein kinase csk , sh2 domain , kinase , protein kinase domain , src family kinase , microbiology and biotechnology , biology , computational biology , biochemistry , gene , mutant
Src-family kinases are modular signaling proteins involved in a diverse array of cellular processes. All members of the Src family share the same domain organization, with modular SH3, SH2 and kinase domains followed by a C-terminal negative regulatory tail. X-ray crystallographic analyses of several Src family members have revealed critical roles for the SH3 and SH2 domains in the down-regulation of the kinase domain. This review focuses on biological, biophysical, and computational studies that reveal conformationally distinct active states within this unique kinase family.