1bui: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1bui |SIZE=350|CAPTION= <scene name='initialview01'>1bui</scene>, resolution 2.65Å | |PDB= 1bui |SIZE=350|CAPTION= <scene name='initialview01'>1bui</scene>, resolution 2.65Å | ||
|SITE= <scene name='pdbsite=ASA:Catalytic+Site+Of+Chain+A'>ASA</scene> and <scene name='pdbsite=ASB:Catalytic+Site+Of+Chain+B'>ASB</scene> | |SITE= <scene name='pdbsite=ASA:Catalytic+Site+Of+Chain+A'>ASA</scene> and <scene name='pdbsite=ASB:Catalytic+Site+Of+Chain+B'>ASB</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MAI:DEOXO-METHYLARGININE'>MAI</scene> | ||
|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=1bui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bui OCA], [http://www.ebi.ac.uk/pdbsum/1bui PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bui RCSB]</span> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
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 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 Structure== | ==About this Structure== | ||
| Line 40: | Line 40: | ||
[[Category: staphylokinase]] | [[Category: staphylokinase]] | ||
''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 19:08:34 2008'' | ||
Revision as of 16:08, 30 March 2008
| |||||||||||||
| 1bui, resolution 2.65Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | ASA and ASB | ||||||||||||
| Ligands: | MAI | ||||||||||||
| Activity: | Plasmin, with EC number 3.4.21.7 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF THE TERNARY MICROPLASMIN-STAPHYLOKINASE-MICROPLASMIN COMPLEX: A PROTEINASE-COFACTOR-SUBSTRATE COMPLEX IN ACTION.
Overview
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 Structure
1BUI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 19:08:34 2008
