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| [[Image:1bui.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1bui| PDB=1bui | SCENE= }} | | {{STRUCTURE_1bui| PDB=1bui | SCENE= }} |
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| '''STRUCTURE OF THE TERNARY MICROPLASMIN-STAPHYLOKINASE-MICROPLASMIN COMPLEX: A PROTEINASE-COFACTOR-SUBSTRATE COMPLEX IN ACTION.'''
| | ===STRUCTURE OF THE TERNARY MICROPLASMIN-STAPHYLOKINASE-MICROPLASMIN COMPLEX: A PROTEINASE-COFACTOR-SUBSTRATE COMPLEX IN ACTION.=== |
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| ==Overview==
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| The serine proteinase plasmin is the key fibrinolytic enzyme that dissolves blood clots and also promotes cell migration and tissue remodeling. Here, we report the 2.65 A crystal structure of a ternary complex of microplasmin-staphylokinase bound to a second microplasmin. The staphylokinase 'cofactor' does not affect the active-site geometry of the plasmin 'enzyme', but instead modifies its subsite specificity by providing additional docking sites for enhanced presentation of the plasminogen 'substrate' to the 'enzymes's' active site. The activation loop of the plasmin 'substrate', cleaved in these crystals, can be reconstructed to show how it runs across the active site of the plasmin 'enzyme' prior to activation cleavage. This is the first experimental structure of a productive proteinase-cofactor-macromolecular substrate complex. Furthermore, it provides a template for the design of improved plasminogen activators and plasmin inhibitors with considerable therapeutical potential. | | The line below this paragraph, {{ABSTRACT_PUBMED_9783753}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9783753 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9783753}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Serine proteinase]] | | [[Category: Serine proteinase]] |
| [[Category: Staphylokinase]] | | [[Category: Staphylokinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:58:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:44:31 2008'' |