1s1d

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[[Image:1s1d.jpg|left|200px]]<br /><applet load="1s1d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s1d.jpg|left|200px]]
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caption="1s1d, resolution 1.60&Aring;" />
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'''Structure and protein design of human apyrase'''<br />
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{{Structure
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|PDB= 1s1d |SIZE=350|CAPTION= <scene name='initialview01'>1s1d</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=GP2:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANOSYL+ESTER'>GP2</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [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]
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|GENE= SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Structure and protein design of human apyrase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1S1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1D OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15006348 15006348]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15006348 15006348]
[[Category: Apyrase]]
[[Category: Apyrase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: nucleotide-binding motif]]
[[Category: nucleotide-binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:10 2008''

Revision as of 11:59, 20 March 2008


PDB ID 1s1d

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: , , , and
Gene: SHAPY (Homo sapiens)
Activity: Apyrase, with EC number 3.6.1.5
Coordinates: save as pdb, mmCIF, xml



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. 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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