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1s1d

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1s1d, resolution 1.60Å ()
Ligands: , , , ,
Gene: SHAPY (Homo sapiens)
Activity: Apyrase, with EC number 3.6.1.5
Related: 1s18
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Structure and protein design of human apyrase

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1s1d is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Dai J, Liu J, Deng Y, Smith TM, Lu M. Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. PMID:15006348

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