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.


1shl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1shl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1shl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1shl| PDB=1shl | SCENE= }}
{{STRUCTURE_1shl| PDB=1shl | SCENE= }}
-
'''CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR'''
+
===CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR===
-
==Overview==
+
<!--
-
Allosteric regulation of proteins by conformational change is a primary means of biological control. Traditionally it has been difficult to identify and characterize novel allosteric sites and ligands that freeze these conformational states. We present a site-directed approach using Tethering for trapping inhibitory small molecules at sites away from the active site by reversible disulfide bond formation. We screened a library of 10,000 thiol-containing compounds against accessible cysteines of two members of the caspase family of proteases, caspase-3 and -7. We discovered a previously unreported and conserved allosteric site in a deep cavity at the dimer interface 14 A from the active site. This site contains a natural cysteine that, when disulfide-bonded with either of two specific compounds, inactivates these proteases. The allosteric site is functionally coupled to the active site, such that binding of the compounds at the allosteric site prevents peptide binding at the active site. The x-ray crystal structures of caspase-7 bound by either compound demonstrates that they inhibit caspase-7 by trapping a zymogen-like conformation. This approach may be useful to identify new allosteric sites from natural or engineered cysteines, to study allosteric transitions in proteins, and to nucleate drug discovery efforts.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15314233}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15314233 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15314233}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Inhibitor]]
[[Category: Inhibitor]]
[[Category: Protease]]
[[Category: Protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:42:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:41:32 2008''

Revision as of 13:41, 27 July 2008

Image:1shl.png

Template:STRUCTURE 1shl

CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR

Template:ABSTRACT PUBMED 15314233

About this Structure

1SHL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Discovery of an allosteric site in the caspases., Hardy JA, Lam J, Nguyen JT, O'Brien T, Wells JA, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12461-6. Epub 2004 Aug 16. PMID:15314233

Page seeded by OCA on Sun Jul 27 16:41:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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