1s1d: Difference between revisions
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'''Structure and protein design of human apyrase'''<br /> | '''Structure and protein design of human apyrase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1S1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, ACT, SO4, GP2 and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1S1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=GP2:'>GP2</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1D OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nucleotide-binding motif]] | [[Category: nucleotide-binding motif]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:51:20 2008'' | ||
Revision as of 14:51, 15 February 2008
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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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