作者: Frank Sicheri , John Kuriyan
DOI: 10.1016/S0959-440X(97)80146-7
关键词: SRC Family Tyrosine Kinase 、 Biochemistry 、 Receptor tyrosine kinase 、 Phosphorylation 、 Proto-oncogene tyrosine-protein kinase Src 、 SH2 domain 、 Tyrosine kinase 、 Chemistry 、 SH3 domain 、 Tyrosine-protein kinase CSK 、 Biophysics
摘要: The crystal structures of three Src-family tyrosine kinases have been determined recently. structure the catalytic domain Lck has in active autophosphorylated state. larger constructs c-Src and Hck, containing SH3, SH2 domains, as well a C-terminal regulatory tail, down-regulated state, phosphorylated tail. A comparison these leads to an unanticipated mechanism for regulation activity by cooperative interactions between SH2, SH3 domains.