1q7a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1q7a.jpg|left|200px]]
{{Seed}}
[[Image:1q7a.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q7a|  PDB=1q7a  |  SCENE=  }}  
{{STRUCTURE_1q7a|  PDB=1q7a  |  SCENE=  }}  


'''Crystal structure of the complex formed between russell's viper phospholipase A2 and an antiinflammatory agent oxyphenbutazone at 1.6A resolution'''
===Crystal structure of the complex formed between russell's viper phospholipase A2 and an antiinflammatory agent oxyphenbutazone at 1.6A resolution===




==Overview==
<!--
Phospholipase A(2) (PLA(2); EC 3.1.1.4) is a key enzyme involved in the production of proinflammatory mediators known as eicosanoids. The binding of the substrate to PLA(2) occurs through a well-formed hydrophobic channel. To determine the viability of PLA(2) as a target molecule for the structure-based drug design against inflammation, arthritis, and rheumatism, the crystal structure of the complex of PLA(2) with a known anti-inflammatory compound oxyphenbutazone (OPB), which has been determined at 1.6 A resolution. The structure has been refined to an R factor of 0.209. The structure contains 1 molecule each of PLA(2) and OPB with 2 sulfate ions and 111 water molecules. The binding studies using surface plasmon resonance show that OPB binds to PLA(2) with a dissociation constant of 6.4 x 10(-8) M. The structure determination has revealed the presence of an OPB molecule at the binding site of PLA(2). It fits well in the binding region, thus displaying a high level of complementarity. The structure also indicates that OPB works as a competitive inhibitor. A large number of hydrophobic interactions between the enzyme and the OPB molecule have been observed. The hydrophobic interactions involving residues Tyr(52) and Lys(69) with OPB are particularly noteworthy. Other residues of the hydrophobic channel such as Leu(3), Phe(5), Met(8), Ile(9), and Ala(18) are also interacting extensively with the inhibitor. The crystal structure clearly reveals that the binding of OPB to PLA(2) is specific in nature and possibly suggests that the basis of its anti-inflammatory effects may be due to its binding to PLA(2) as well.
The line below this paragraph, {{ABSTRACT_PUBMED_15544328}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15544328 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15544328}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Phospholipase a2]]
[[Category: Phospholipase a2]]
[[Category: Venom]]
[[Category: Venom]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:57:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:38:15 2008''

Revision as of 04:38, 28 July 2008

File:1q7a.png

Template:STRUCTURE 1q7a

Crystal structure of the complex formed between russell's viper phospholipase A2 and an antiinflammatory agent oxyphenbutazone at 1.6A resolution

Template:ABSTRACT PUBMED 15544328

About this Structure

1Q7A is a Single protein structure of sequence from Daboia russellii russellii. Full crystallographic information is available from OCA.

Reference

Phospholipase A2 as a target protein for nonsteroidal anti-inflammatory drugs (NSAIDS): crystal structure of the complex formed between phospholipase A2 and oxyphenbutazone at 1.6 A resolution., Singh N, Jabeen T, Somvanshi RK, Sharma S, Dey S, Singh TP, Biochemistry. 2004 Nov 23;43(46):14577-83. PMID:15544328

Page seeded by OCA on Mon Jul 28 07:38:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1q7a&oldid=688065"