Crystal structure of streptokinase β-domain

被引：30
作者：
Wang, XQ
Tang, J
Hunter, B
Zhang, XJC
机构：
[1] Oklahoma Med Res Fdn, Crystallog Program, Oklahoma City, OK 73104 USA
[2] Oklahoma Med Res Fdn, Prot Studies Program, Oklahoma City, OK 73104 USA
[3] Univ Oklahoma, Hlth Sci Ctr, Dept Biochem & Mol Biol, Oklahoma City, OK 73104 USA
来源：
FEBS LETTERS | 1999年 / 459卷 / 01期
关键词：
streptokinase; plasminogen; beta-grasp folding; crystal structure;
D O I：
10.1016/S0014-5793(99)01214-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Streptokinase, a 47 kDa secreted protein of hemolytic strains of streptococci, is a human plasminogen activator and contains three structural domains linked by flexible loops. We describe here the crystal structure of the isolated streptokinase middle (SK beta) domain determined at 2.4 Angstrom resolution, Among the functionally important structural features is a putative binding site for a kringle domain of plasminogen located at the tip of a fully exposed hairpin loop. The distribution of genetically conserved residues of SK beta is strongly correlated with their functions. The extensive interface of the SK beta dimer suggests that such dimers may also exist in solution for free SK beta. (C) 1999 Federation of European Biochemical Societies.
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收藏
页码：85 / 89
页数：5
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