Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: Function of His43 and Tyr44

被引：9

作者：

Dahiya, Monika ^{[1
]}

Singh, Satish ^{[1
]}

Rajamohan, Govindan ^{[1
]}

Sethi, Deepti ^{[1
]}

Ashish ^{[1
]}

Dikshit, Kanak L. ^{[1
]}

机构：

[1] CSIR, Inst Microbial Technol, Chandigarh 160036, India

来源：

FEBS LETTERS | 2011年 / 585卷 / 12期

关键词：

Staphylokinase; Plasminogen-activation; Molecular-modeling; Site-directed mutagenesis; Enzyme-substrate complex; Protein-protein interaction; HUMAN PLASMINOGEN; SUBSTRATE COMPLEX; CRYSTAL-STRUCTURE; ACTIVATION; PARTICIPATION; STREPTOKINASE; MECHANISM; MODEL;

D O I：

10.1016/j.febslet.2011.04.030

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：

Staphylokinase (SAK) forms a 1: 1 stoichiometric complex with human plasmin ( Pm) and switches its substrate specificity to generate a plasminogen (Pg) activator complex. Site-directed mutagenesis of SAKHis43 and SAKTyr44 demonstrated the crucial requirement of a positively charged and an aromatic residue, respectively, at these positions for optimal functioning of SAK-Pm activator complex. Molecular modeling studies further revealed the role of these residues in making cation-pi and pi-pi interactions with Trp215 of Pm and thus establishing the crucial intermolecular contacts within the active site cleft of the activator complex for the cofactor activity of SAK. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1814 / 1820

页数：7

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