1bda
From Proteopedia
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| - | [[Image:1bda.gif|left|200px]] | + | [[Image:1bda.gif|left|200px]] |
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| - | '''CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)''' | + | {{Structure |
| + | |PDB= 1bda |SIZE=350|CAPTION= <scene name='initialview01'>1bda</scene>, resolution 3.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CH2:METHYLENE GROUP'>CH2</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/T-plasminogen_activator T-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 3.4.21.68] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BDA is a [ | + | 1BDA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDA OCA]. |
==Reference== | ==Reference== | ||
| - | Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA., Renatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W, EMBO J. 1997 Aug 15;16(16):4797-805. PMID:[http:// | + | Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA., Renatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W, EMBO J. 1997 Aug 15;16(16):4797-805. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9305622 9305622] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Renatus, M.]] | [[Category: Renatus, M.]] | ||
[[Category: CH2]] | [[Category: CH2]] | ||
| - | [[Category: fibrinolytic | + | [[Category: fibrinolytic enzyme]] |
| - | [[Category: plasminogen | + | [[Category: plasminogen activator]] |
[[Category: trypsin like serine protease]] | [[Category: trypsin like serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:28 2008'' |
Revision as of 08:09, 20 March 2008
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| , resolution 3.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | T-plasminogen activator, with EC number 3.4.21.68 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)
Contents |
Overview
Tissue type plasminogen activator (tPA) is the physiological initiator of fibrinolysis, activating plasminogen via highly specific proteolysis; plasmin then degrades fibrin with relatively broad specificity. Unlike other chymotrypsin family serine proteinases, tPA is proteolytically active in a single-chain form. This form is also preferred for therapeutic administration of tPA in cases of acute myocardial infarction. The proteolytic cleavage which activates most other chymotrypsin family serine proteinases increases the catalytic efficiency of tPA only 5- to 10-fold. The X-ray crystal structure of the catalytic domain of recombinant human single-chain tPA shows that Lys156 forms a salt bridge with Asp194, promoting an active conformation in the single-chain form. Comparisons with the structures of other serine proteinases that also possess Lys156, such as trypsin, factor Xa and human urokinase plasminogen activator (uPA), identify a set of secondary interactions which are required for Lys156 to fulfil this activating role. These findings help explain the anomalous single-chain activity of tPA and may suggest strategies for design of new therapeutic plasminogen activators.
Disease
Known disease associated with this structure: Plasminogen activator deficiency OMIM:[173370]
About this Structure
1BDA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA., Renatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W, EMBO J. 1997 Aug 15;16(16):4797-805. PMID:9305622
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