Crystal structure of the Src family tyrosine kinase Hck
Crystal structure of the Src family tyrosine kinase Hck
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DOI：
10.1038/385602a0
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发表时间：
1997-02-13
期刊：
影响因子：
64.8
通讯作者：
Kuriyan, J
中科院分区：
文献类型：
--
作者：
Sicheri, F;Moarefi, I;Kuriyan, J
已在2.6/2.9埃分辨率下测定了造血细胞激酶Hck的晶体结构。酶活性的抑制是酶的Src同源结构域SH 2和SH 3的分子内相互作用的结果，伴随着催化结构域的元件的置换。活性位点的构象与非活性细胞周期蛋白依赖性蛋白激酶的构象相似。
The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Angstrom resolution. Inhibition of enzymatic activity is a consequence of intramolecular interactions of the enzyme's Src-homology domains SH2 and SH3, with concomitant displacement of elements of the catalytic domain. The conformation of the active site has similarities with that of Inactive cyclln-dependent protein kinases.