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.


1fs4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fs4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fs4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fs4| PDB=1fs4 | SCENE= }}
{{STRUCTURE_1fs4| PDB=1fs4 | SCENE= }}
-
'''Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design'''
+
===Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design===
-
==Overview==
+
<!--
-
Glycogen phosphorylase (GP) is currently exploited as a target for inhibition of hepatic glycogenolysis under high glucose conditions. Spirohydantoin of glucopyranose and N-acetyl-beta-D-glucopyranosylamine have been identified as the most potent inhibitors of GP that bind at the catalytic site. Four spirohydantoin and three beta-D-glucopyranosylamine analogs have been designed, synthesized and tested for inhibition of GP in kinetic experiments. Depending on the functional group introduced, the K(i) values varied from 16.5 microM to 1200 microM. In order to rationalize the kinetic results, we determined the crystal structures of the analogs in complex with GP. All the inhibitors bound at the catalytic site of the enzyme, by making direct and water-mediated hydrogen bonds with the protein and by inducing minor movements of the side chains of Asp283 and Asn284, of the 280s loop that blocks access of the substrate glycogen to the catalytic site, and changes in the water structure in the vicinity of the site. The differences observed in the Ki values of the analogs can be interpreted in terms of variations in hydrogen bonding and van der Waals interactions, desolvation effects, ligand conformational entropy, and displacement of water molecules on ligand binding to the catalytic site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16222658}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16222658 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16222658}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Zographos, S E.]]
[[Category: Zographos, S E.]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Enzyme-inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:42:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:51:41 2008''

Revision as of 00:51, 1 July 2008

Image:1fs4.png

Template:STRUCTURE 1fs4

Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design

Template:ABSTRACT PUBMED 16222658

About this Structure

1FS4 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Kinetic and crystallographic studies of glucopyranose spirohydantoin and glucopyranosylamine analogs inhibitors of glycogen phosphorylase., Watson KA, Chrysina ED, Tsitsanou KE, Zographos SE, Archontis G, Fleet GW, Oikonomakos NG, Proteins. 2005 Dec 1;61(4):966-83. PMID:16222658

Page seeded by OCA on Tue Jul 1 03:51:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fs4"
Personal tools