Recognition and specificity in protein tyrosine kinase-mediated signalling
Recognition and specificity in protein tyrosine kinase-mediated signalling
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DOI：
10.1016/s0968-0004(00)89103-3
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发表时间：
1995-01-01
影响因子：
13.8
通讯作者：
Cantley, Lewis C.
中科院分区：
文献类型：
--
作者：
Songyang, Zhou;Cantley, Lewis C.
有几个因素导致蛋白酪氨酸激酶(PTK)在信号转导途径中的特异性。虽然蛋白质-蛋白质相互作用结构域，如Src同源结构域(SH2和SH3)调节PTKs及其底物的细胞定位，但PTKs的特异性最终取决于它们的催化结构域。多肽文库的使用揭示了SH2结构域和PTK催化结构域的底物特异性，并提示了这些结构域之间的串扰。
There are several factors that contribute to the specificities of protein tyrosine kinases (PTKs) in signal transduction pathways. While protein-protein interaction domains, such as the Src homology (SH2 and SH3) domains, regulate the cellular localization of PTKs and their substrates, the specificities of PTKs are ultimately determined by their catalytic domains. The use of peptide libraries has revealed the substrate specificities of SH2 domains and PTK catalytic domains, and has suggested cross-talk between these domains.