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

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44.
 
Creator Dahiya, Monika
Singh, Satish
Rajamohan, Govindan
Sethi, Deepti
Ganguly, Ashish
Dikshit, Kanak L
 
Subject QR Microbiology
 
Description 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.
 
Publisher Elsevier Science
 
Date 2011-06-23
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/471/1/dikshit11.1.pdf
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
 
Relation http://www.sciencedirect.com/science/article/pii/S0014579311002778
http://crdd.osdd.net/open/471/