Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: Function of His43 and Tyr44
Copyright policy )Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: Function of His43 and Tyr44
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.
Models, Molecular, Site-directed mutagenesis, Binding Sites, Metalloendopeptidases, Enzyme–substrate complex, Electrons, Plasminogen, Molecular-modeling, Substrate Specificity, Protein–protein interaction, Escherichia coli, Mutagenesis, Site-Directed, Humans, Tyrosine, Staphylokinase, Plasminogen-activation, Histidine, Fibrinolysin, Protein Binding
Models, Molecular, Site-directed mutagenesis, Binding Sites, Metalloendopeptidases, Enzyme–substrate complex, Electrons, Plasminogen, Molecular-modeling, Substrate Specificity, Protein–protein interaction, Escherichia coli, Mutagenesis, Site-Directed, Humans, Tyrosine, Staphylokinase, Plasminogen-activation, Histidine, Fibrinolysin, Protein Binding
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