Crystal structure of the Src family tyrosine kinase Hck

被引：1038

作者：

Sicheri, F

Moarefi, I

Kuriyan, J

机构：

[1] ROCKEFELLER UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA

[2] ROCKEFELLER UNIV, LAB MOL BIOPHYS, NEW YORK, NY 10021 USA

来源：

NATURE | 1997年 / 385卷 / 6617期

关键词：

D O I：

10.1038/385602a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

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页码：602 / 609

页数：8

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