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

Dahiya, Monika and Singh, Satish and Rajamohan, Govindan and Sethi, Deepti and Ganguly, Ashish and Dikshit, Kanak L (2011) Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44. FEBS letters, 585 (12). pp. 1814-20. ISSN 1873-3468

PDF dikshit11.1.pdf - Published Version Restricted to Registered users only Download (1170Kb) | Request a copy

Abstract

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.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Science
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	09 Dec 2011 06:56
Last Modified:	22 Jul 2015 03:54
URI:	http://crdd.osdd.net/open/id/eprint/471

Actions (login required)

View Item