2fqq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2fqq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2fqq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fqq| PDB=2fqq | SCENE= }}
{{STRUCTURE_2fqq| PDB=2fqq | SCENE= }}
-
'''Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide'''
+
===Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide===
-
==Overview==
+
<!--
-
We present a common allosteric mechanism for control of inflammatory and apoptotic caspases. Highly specific thiol-containing inhibitors of the human inflammatory caspase-1 were identified by using disulfide trapping, a method for site-directed small-molecule discovery. These compounds became trapped by forming a disulfide bond with a cysteine residue in the cavity at the dimer interface approximately 15 A away from the active site. Mutational and structural analysis uncovered a linear circuit of functional residues that runs from one active site through the allosteric cavity and into the second active site. Kinetic analysis revealed robust positive cooperativity not seen in other endopeptidases. Recently, disulfide trapping identified a similar small-molecule site and allosteric transition in the apoptotic caspase-7 that shares only a 23% sequence identity with caspase-1. Together, these studies show a general small-molecule-binding site for functionally reversing the zymogen activation of caspases and suggest a common regulatory site for the allosteric control of inflammation and apoptosis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16682620}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16682620 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16682620}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Allosteric inhibitor]]
[[Category: Allosteric inhibitor]]
[[Category: Caspase]]
[[Category: Caspase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:12:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:44:03 2008''

Revision as of 11:44, 29 July 2008

Image:2fqq.png

Template:STRUCTURE 2fqq

Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala) in complex with 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide

Template:ABSTRACT PUBMED 16682620

About this Structure

2FQQ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A common allosteric site and mechanism in caspases., Scheer JM, Romanowski MJ, Wells JA, Proc Natl Acad Sci U S A. 2006 May 16;103(20):7595-600. Epub 2006 May 8. PMID:16682620

Page seeded by OCA on Tue Jul 29 14:44:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fqq"
Personal tools