Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
View Archive Info| Field | Value | |
| Title |
Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44.
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| Creator |
Dahiya, Monika
Singh, Satish Rajamohan, Govindan Sethi, Deepti Ganguly, Ashish Dikshit, Kanak L |
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| Subject |
QR Microbiology
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| 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.
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| Publisher |
Elsevier Science
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| Date |
2011-06-23
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| 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 |
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| Relation |
http://www.sciencedirect.com/science/article/pii/S0014579311002778
http://crdd.osdd.net/open/471/ |
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