1s1d

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Revision as of 17:02, 12 November 2007

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spinqualitylabelsall models 1s1d, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with CA, ACT, SO4, GP2 and TRS as ligands. Active as Apyrase, with EC number 3.6.1.5 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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