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1bml
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bml OCA], [http://www.ebi.ac.uk/pdbsum/1bml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bml RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Plasminogen Tochigi disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Plasminogen deficiency, types I and II OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]], Thrombophilia, dysplasminogenemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173350 173350]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: streptokinase]] | [[Category: streptokinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:03:56 2008'' |
Revision as of 16:04, 30 March 2008
| |||||||
| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Plasmin, with EC number 3.4.21.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE
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.
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 Sun Mar 30 19:03:56 2008
