Pro⁴² and Val⁴⁵ of staphylokinase modulate intermolecular interactions of His⁴³-Tyr⁴⁴ pair and specificity of staphylokinase-plasmin activator complex

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• 作者：Satish Singh ; Ashish ; Kanak L. Dikshit ; ^{kanak@imtech.res.in}
• 关键词：Staphylokinase ; Plasminogen activation ; Molecular modeling ; Site-directed mutagenesis ; Enzyme&ndash ; substrate complex ; Protein&ndash ; protein interaction
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：23 March, 2012
• 卷：586
• 期：6
• 页码：653-658
• 文件大小：715 K

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 His⁴³-Tyr⁴⁴ 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 His⁴³ with Trp²¹⁵ of partner Pm within the active site, whereas pi-pi interaction of Tyr⁴⁴ with Trp²¹⁵ remain energetically favoured.

Structured summary of protein interactions

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