Sicheri F, Moarefi I, Kuriyan J
Laboratories of Molecular Biophysics, The Rockefeller University, New York 10021, USA.
Nature. 1997 Feb 13;385(6617):602-9. doi: 10.1038/385602a0.
The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 A 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 cyclin-dependent protein kinases.
造血细胞激酶Hck的晶体结构已在2.6/2.9埃分辨率下测定。酶活性的抑制是该酶的Src同源结构域SH2和SH3分子内相互作用的结果，同时催化结构域的元件发生位移。活性位点的构象与无活性的细胞周期蛋白依赖性蛋白激酶的构象相似。
