This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1s18
From Proteopedia
(New page: 200px<br /> <applet load="1s18" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s18, resolution 1.70Å" /> '''Structure and prote...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1s18.gif|left|200px]]<br /> | + | [[Image:1s18.gif|left|200px]]<br /><applet load="1s18" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1s18" size=" | + | |
caption="1s18, resolution 1.70Å" /> | caption="1s18, resolution 1.70Å" /> | ||
'''Structure and protein design of human apyrase'''<br /> | '''Structure and protein design of human apyrase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hematophagous arthropods secrete a salivary apyrase that inhibits platelet | + | 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== | ==About this Structure== | ||
| - | 1S18 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 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:// | + | 1S18 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> 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=1S18 OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 18: | ||
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
| - | [[Category: Smith, T | + | [[Category: Smith, T M.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CA]] | [[Category: CA]] | ||
| Line 28: | Line 27: | ||
[[Category: nucleotide-binding motif]] | [[Category: nucleotide-binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:48 2008'' |
Revision as of 12:56, 21 February 2008
|
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
1S18 is a Single protein structure of sequence from Homo sapiens with , and 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
Page seeded by OCA on Thu Feb 21 14:56:48 2008
Categories: Apyrase | Homo sapiens | Single protein | Dai, J. | Deng, Y. | Liu, J. | Lu, M. | Smith, T M. | ACT | CA | TRS | Adpase | Calcium-binding protein | Five-blade beta propeller | Nucleotide-binding motif
