1bui
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STRUCTURE OF THE TERNARY MICROPLASMIN-STAPHYLOKINASE-MICROPLASMIN COMPLEX: A PROTEINASE-COFACTOR-SUBSTRATE COMPLEX IN ACTION.
OverviewOverview
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.
About this StructureAbout this Structure
1BUI is a Protein complex structure of sequences from Homo sapiens. Active as Plasmin, with EC number 3.4.21.7 Structure known Active Sites: ASA and ASB. Full crystallographic information is available from OCA.
ReferenceReference
The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action., Parry MA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Guhrs KH, Bode W, Nat Struct Biol. 1998 Oct;5(10):917-23. PMID:9783753
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