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.


1pge

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pge.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1pge.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pge| PDB=1pge | SCENE= }}
{{STRUCTURE_1pge| PDB=1pge | SCENE= }}
-
'''PROSTAGLANDIN H2 SYNTHASE-1 COMPLEXED WITH P-(2'-IODO-5'-THENOYL)HYDROTROPIC ACID (IODOSUPROFEN)'''
+
===PROSTAGLANDIN H2 SYNTHASE-1 COMPLEXED WITH P-(2'-IODO-5'-THENOYL)HYDROTROPIC ACID (IODOSUPROFEN)===
-
==Overview==
+
<!--
-
The cyclooxygenase activity of the membrane protein prostaglandin H2 synthase isoform 1 (PGHS-1) is the target of the nonsteroidal antiinflammatory drugs (NSAIDs). The X-ray crystal structures of PGHS-1 in complex with the NSAIDs flurbiprofen and bromoaspirin have been determined previously [Picot, D., et al. (1994) Nature 367, 243-249; Loll, P. J., et al. (1995) Nat. Struct. Biol. 2, 637-643]. We report here the preparation and characterization of novel potent iodinated analogs of the NSAIDs indomethacin and suprofen, as well as the refined X-ray crystal structures of their complexes with PGHS-1. The PGHS-iodosuprofen complex structure has been refined at 3.5 A to an R-value of 0.189 and shows the suprofen analog to share a common mode of binding with flurbiprofen. The PGHS-iodoindomethacin complex structure has been refined at 4.5 A to an R-value of 0.254. The low resolution of the iodoindomethacin complex structure precludes detailed modeling of drug-enzyme interactions, but the electron-dense iodine atom of the inhibitor has been unambiguously located, allowing for the placement and approximate orientation of the inhibitor in the enzyme's active site. We have modeled two equally likely binding modes for iodoindomethacin, corresponding to the two principal conformers of the inhibitor. Like flurbiprofen, iodosuprofen and iodoindomethacin bind at the end of the long channel which leads into the enzyme active site. Binding at this site presumably blocks access of substrate to Tyr-385, a residue essential for catalysis. No evidence is seen for significant protein conformational differences between the iodoindomethacin and iodosuprofen of flurbiprofen complex structures.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8652509}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8652509 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8652509}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:03:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:35:54 2008''

Revision as of 01:35, 29 July 2008

Image:1pge.png

Template:STRUCTURE 1pge

PROSTAGLANDIN H2 SYNTHASE-1 COMPLEXED WITH P-(2'-IODO-5'-THENOYL)HYDROTROPIC ACID (IODOSUPROFEN)

Template:ABSTRACT PUBMED 8652509

About this Structure

1PGE is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.

Reference

Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the prostaglandin H2 synthase cyclooxygenase active site., Loll PJ, Picot D, Ekabo O, Garavito RM, Biochemistry. 1996 Jun 11;35(23):7330-40. PMID:8652509

Page seeded by OCA on Tue Jul 29 04:35:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pge"
Personal tools