2q61: Difference between revisions

Revision as of 12:50, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2q61.png

Template:STRUCTURE 2q61

Crystal Structure of PPARgamma ligand binding domain bound to partial agonist SR145Crystal Structure of PPARgamma ligand binding domain bound to partial agonist SR145

Template:ABSTRACT PUBMED 17937915

About this StructureAbout this Structure

2Q61 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Partial agonists activate PPARgamma using a helix 12 independent mechanism., Bruning JB, Chalmers MJ, Prasad S, Busby SA, Kamenecka TM, He Y, Nettles KW, Griffin PR, Structure. 2007 Oct;15(10):1258-71. PMID:17937915

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OCA

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-'''Crystal Structure of PPARgamma ligand binding domain bound to partial agonist SR145'''
+===Crystal Structure of PPARgamma ligand binding domain bound to partial agonist SR145===
-==Overview==
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-Binding to helix 12 of the ligand-binding domain of PPARgamma is required for full agonist activity. Previously, the degree of stabilization of the activation function 2 (AF-2) surface was thought to correlate with the degree of agonism and transactivation. To examine this mechanism, we probed structural dynamics of PPARgamma with agonists that induced graded transcriptional responses. Here we present crystal structures and amide H/D exchange (HDX) kinetics for six of these complexes. Amide HDX revealed each ligand induced unique changes to the dynamics of the ligand-binding domain (LBD). Full agonists stabilized helix 12, whereas intermediate and partial agonists did not at all, and rather differentially stabilized other regions of the binding pocket. The gradient of PPARgamma transactivation cannot be accounted for solely through changes to the dynamics of AF-2. Thus, our understanding of allosteric signaling must be extended beyond the idea of a dynamic helix 12 acting as a molecular switch.
+The line below this paragraph, {{ABSTRACT_PUBMED_17937915}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17937915}}
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 [[Category: Ligand binding protein]]
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