1s18: Difference between revisions

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[[Image:1s18.gif|left|200px]]
{{Seed}}
[[Image:1s18.png|left|200px]]


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{{STRUCTURE_1s18|  PDB=1s18  |  SCENE=  }}  
{{STRUCTURE_1s18|  PDB=1s18  |  SCENE=  }}  


'''Structure and protein design of human apyrase'''
===Structure and protein design of human apyrase===




==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: Adpase,five-blade beta propeller,calcium-binding protein]]
[[Category: Adpase,five-blade beta propeller,calcium-binding protein]]
[[Category: Nucleotide-binding motif]]
[[Category: Nucleotide-binding motif]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:10:01 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:41:52 2008''

Revision as of 09:41, 27 July 2008

File:1s18.png

Template:STRUCTURE 1s18

Structure and protein design of human apyrase

Template:ABSTRACT PUBMED 15006348

About this Structure

1S18 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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