2v95: Difference between revisions

Revision as of 14:40, 29 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.

Template:STRUCTURE 2v95

STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOLSTRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL

Template:ABSTRACT PUBMED 17644521

About this StructureAbout this Structure

2V95 is a Single protein structure of sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 2v6d. Full crystallographic information is available from OCA.

ReferenceReference

Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release., Klieber MA, Underhill C, Hammond GL, Muller YA, J Biol Chem. 2007 Oct 5;282(40):29594-603. Epub 2007 Jul 19. PMID:17644521

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OCA

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-'''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL'''
+===STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL===
-==Overview==
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-Corticosteroid-binding globulin (CBG) is a serine proteinase inhibitor (serpin) family member that transports glucocorticoids in blood and regulates their access to target cells. The 1.9A crystal structure of rat CBG shows that its steroid-binding site resembles the thyroxin-binding site in the related serpin, thyroxin-binding globulin, and mutagenesis studies have confirmed the contributions of key residues that constitute the steroid-binding pocket. Unlike thyroxin-bound thyroxin-binding globulin, the cortisol-bound CBG displays an "active" serpin conformation with the proteinase-sensitive, reactive center loop (RCL) fully expelled from the regulatory beta-sheet A. Moreover, the CBG structure allows us to predict that complete insertion of the proteolytically cleaved RCL into the serpin fold occurs in concert with a displacement and unwinding of helix D that would disrupt the steroid-binding site. This allosteric coupling between RCL positioning and occupancy of the CBG steroid-binding site, which resembles the ligand (glycosamino-glycan)-dependent activation of the thrombin inhibitory serpins heparin cofactor II and anti-thrombin RCLs, ensures both optimal recognition of CBG by target proteinases and efficient release of steroid to sites of action.
+The line below this paragraph, {{ABSTRACT_PUBMED_17644521}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Steroid-binding]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:24:38 2008''
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