Pro(42) and Val(45) of staphylokinase modulate intermolecular interactions of His(43)-Tyr(44) pair and specificity of staphylokinase-plasmin activator complex

[摘要]：Staphylokinase (SAK) forms a 1:1 stoichiometric complex with plasmin (Pm) and changes its substrate specificity to create a plasminogen (Pg) activator complex. The His(43)-Tyr(44) pair of SAK resides within the active site cleft of the partner Pm and generates intermolecular contacts to confer Pg activator ability to the SAK-Pm bimolecular complex. Site-directed mutagenesis and molecular modeling studies unravelled that mutation at 42nd or 45th positions of SAK specifically disrupts cation-pi interaction of His(43) with Trp(215) of partner Pm within the active site, whereas pi-pi interaction of Tyr(44) with Trp(215) remain energetically favoured. Structured summary of protein interactions: Pg binds to SAK by surface plasmon resonance (View Interaction: 1, 2, 3) SAK enzymaticly reacts Pg by enzymatic study (View Interaction: 1, 2, 3, 4, 5) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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