This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1s1d
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[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]] | ||
| Line 38: | Line 36: | ||
[[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
