1s1d
From Proteopedia
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|PDB= 1s1d |SIZE=350|CAPTION= <scene name='initialview01'>1s1d</scene>, resolution 1.60Å | |PDB= 1s1d |SIZE=350|CAPTION= <scene name='initialview01'>1s1d</scene>, resolution 1.60Å | ||
|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=GP2:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANOSYL+ESTER'>GP2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=[[1s18|1S18]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1d OCA], [http://www.ebi.ac.uk/pdbsum/1s1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s1d RCSB]</span> | ||
}} | }} | ||
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[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Smith, T M.]] | [[Category: Smith, T M.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GP2]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: TRS]] | ||
[[Category: adpase]] | [[Category: adpase]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
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[[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 23:35:59 2008'' |
Revision as of 20:36, 30 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | SHAPY (Homo sapiens) | ||||||
| Activity: | Apyrase, with EC number 3.6.1.5 | ||||||
| Related: | 1S18
| ||||||
| 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
1S1D 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
Page seeded by OCA on Sun Mar 30 23:35:59 2008
