1s1d

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{{STRUCTURE_1s1d| PDB=1s1d | SCENE= }}
{{STRUCTURE_1s1d| PDB=1s1d | SCENE= }}
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'''Structure and protein design of human apyrase'''
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===Structure and protein design of human apyrase===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15006348}}
==About this Structure==
==About this Structure==
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[[Category: Five-blade beta propeller]]
[[Category: Five-blade beta propeller]]
[[Category: Nucleotide-binding motif]]
[[Category: Nucleotide-binding motif]]
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Revision as of 21:40, 27 July 2008

Image:1s1d.png

Template:STRUCTURE 1s1d

Structure and protein design of human apyrase

Template:ABSTRACT PUBMED 15006348

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

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