1s18: Difference between revisions
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|PDB= 1s18 |SIZE=350|CAPTION= <scene name='initialview01'>1s18</scene>, resolution 1.70Å | |PDB= 1s18 |SIZE=350|CAPTION= <scene name='initialview01'>1s18</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </span> | ||
|GENE= SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1s1d|1S1D]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s18 OCA], [http://www.ebi.ac.uk/pdbsum/1s18 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s18 RCSB]</span> | |||
}} | }} | ||
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[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Smith, T M.]] | [[Category: Smith, T M.]] | ||
[[Category: adpase,five-blade beta propeller,calcium-binding protein]] | |||
[[Category: adpase | |||
[[Category: nucleotide-binding motif]] | [[Category: nucleotide-binding motif]] | ||
''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 23:35:53 2008'' | ||
Revision as of 20:35, 30 March 2008
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| 1s18, resolution 1.70Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ACT, CA, TRS | ||||||||||||
| Gene: | SHAPY (Homo sapiens) | ||||||||||||
| Activity: | Apyrase, with EC number 3.6.1.5 | ||||||||||||
| Related: | 1S1D
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure and protein design of human apyrase
Overview
Hematophagous arthropods secrete a salivary apyrase that inhibits platelet activation by catabolizing ADP released from damaged tissues and blood cells. We report the X-ray crystal structures of a human enzyme of the soluble apyrase family in its apo state and bound to a substrate analog. The structures reveal a nucleotide binding domain comprising a five-blade beta propeller, binding determinants of the substrate and the active site, and an unusual calcium binding site with a potential regulatory function. Using a comparative structural biology approach, we were able to redesign the human apyrase so as to enhance its ADPase activity by more than 100-fold. The engineered enzyme is a potent inhibitor of platelet aggregation and may serve as the basis for the development of a new class of antithrombotic agents.
About this Structure
1S18 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and protein design of a human platelet function inhibitor., Dai J, Liu J, Deng Y, Smith TM, Lu M, Cell. 2004 Mar 5;116(5):649-59. PMID:15006348
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