Singh, Satish and Ganguly, Ashish and Dikshit, Kanak L (2012) Pro42 and Val45 of staphylokinase modulate intermolecular interactions of His43-Tyr44 pair and specificity of staphylokinase-plasmin activator complex. FEBS letters, 586 (6). pp. 653-8. ISSN 1873-3468
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Abstract
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.
Item Type: | Article |
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Additional Information: | Copyright of this article belongs to Elsevier Science. |
Uncontrolled Keywords: | Staphylokinase; Plasminogen activation;Molecular modeling; Site-directed mutagenesis; Enzyme–substrate complex; Protein–protein interaction. |
Subjects: | Q Science > QR Microbiology |
Depositing User: | Dr. K.P.S.Sengar |
Date Deposited: | 28 Jan 2013 06:37 |
Last Modified: | 22 Jul 2015 03:38 |
URI: | http://crdd.osdd.net/open/id/eprint/1264 |
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