1oxr: Difference between revisions

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


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{{STRUCTURE_1oxr|  PDB=1oxr  |  SCENE=  }}  
{{STRUCTURE_1oxr|  PDB=1oxr  |  SCENE=  }}  


'''Aspirin induces its Anti-inflammatory effects through its specific binding to Phospholipase A2: Crystal structure of the complex formed between Phospholipase A2 and Aspirin at 1.9A resolution'''
===Aspirin induces its Anti-inflammatory effects through its specific binding to Phospholipase A2: Crystal structure of the complex formed between Phospholipase A2 and Aspirin at 1.9A resolution===




==Overview==
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Phospholipase A2 is potentially an important target for structure-based rational drug design. In order to determine the involvement of phospholipase A2 in the action of non-steroidal anti-inflammatory drugs (NSAIDs), the crystal structure of the complex formed between phospholipase A2 and aspirin has been determined at 1.9 angstroms resolution. The structure contains 915 protein atoms, 1 calcium ion, 13 atoms of aspirin and 105 water molecules. The observed electron density of the aspirin molecule in the structure was of very high quality thus allowing the precise determination of its atomic coordinates leading to the clear description of its interactions with the enzyme. The structure of the complex clearly shows that aspirin is literally embedded in the hydrophobic environment of PLA2. It is so placed in the substrate binding channel that it forms several important attractive interactions with calcium ion, His 48 and Asp 49. Thus, the structure of the complex clearly shows that aspirin occupies a favourable place in the specific binding site of PLA2. The binding studies have shown that acetyl salicylate (aspirin) binds to PLA2 enzyme specifically with a dissociation constant of 6.4 x 10(-6) M. The structural details and binding data suggest that the inhibition of PLA2 by aspirin is of pharmacological
The line below this paragraph, {{ABSTRACT_PUBMED_15823962}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15823962 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15823962}}


==About this Structure==
==About this Structure==
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[[Category: O-acetyl-oxy phenol]]
[[Category: O-acetyl-oxy phenol]]
[[Category: Pla2]]
[[Category: Pla2]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:24:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:40:49 2008''

Revision as of 15:40, 28 July 2008

File:1oxr.gif

Template:STRUCTURE 1oxr

Aspirin induces its Anti-inflammatory effects through its specific binding to Phospholipase A2: Crystal structure of the complex formed between Phospholipase A2 and Aspirin at 1.9A resolution

Template:ABSTRACT PUBMED 15823962

About this Structure

1OXR is a Single protein structure of sequence from Naja sagittifera. Full crystallographic information is available from OCA.

Reference

Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A2: crystal structure of the complex formed between phospholipase A2 and aspirin at 1.9 angstroms resolution., Singh RK, Ethayathulla AS, Jabeen T, Sharma S, Kaur P, Singh TP, J Drug Target. 2005 Feb;13(2):113-9. PMID:15823962

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