Regulation of antigen receptor function by protein tyrosine kinases.
Regulation of antigen receptor function by protein tyrosine kinases.
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蛋白酪氨酸激酶调节抗原受体功能。
DOI：
10.1016/s0079-6107(98)00060-1
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Chan,AC
中科院分区：
文献类型：
--
作者：
Bubeck-Wardenburg,J;Wong,J;Futterer,K;Pappu,R;Fu,C;Waksman,G;Chan,AC
Ligand engagement of membrane receptors activates a program of biochemical events that regulates cellular functions and fates. Studies of growth factor receptors (GFRs), such as the epidermal and platelet derived GFRs, have established a paradigm for growth factor dependent signaling in which ligand binding induced receptor dimerization and thereby permits transphosphorylation and activation of the receptor encoded tyrosine kinases (Schlessinger, 1997). Insights into the mechanistic basis for this activation process have been provided by the solution of the crystal structures encoding the kinase domains of the insulin and fibroblast GFRs (Hubbard et al., 1994; Mohammadi et al., 1997). These structures reveal that phosphorylation of tyrosine residues within the trans-activation (T) loop of the catalytic domain induces conformational changes which stabilize the activated conformation thereby increasing enzymatic activity. Activation, in turn, results in phosphorylation of additional tyrosine residues encoded within the receptors' cytoplasmic domains facilitating the recruitment of SH2 and PTB domain containing effector and adaptor molecules (Pawson and Scott, 1997;
