1bml
From Proteopedia
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| , resolution 2.9Å | |||||||
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| Activity: | Plasmin, with EC number 3.4.21.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE
Contents |
Overview
Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.
Disease
Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]
About this Structure
1BML is a Protein complex structure of sequences from Homo sapiens and Streptococcus dysgalactiae subsp. equisimilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human plasmin complexed with streptokinase., Wang X, Lin X, Loy JA, Tang J, Zhang XC, Science. 1998 Sep 11;281(5383):1662-5. PMID:9733510
Page seeded by OCA on Thu Mar 20 10:13:01 2008
