2v95
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v95 OCA], [http://www.ebi.ac.uk/pdbsum/2v95 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v95 RCSB]</span> | ||
}} | }} | ||
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[[Category: Klieber, M A.]] | [[Category: Klieber, M A.]] | ||
[[Category: Muller, Y A.]] | [[Category: Muller, Y A.]] | ||
| - | [[Category: PDN]] | ||
[[Category: cbg]] | [[Category: cbg]] | ||
[[Category: corticosteroid-binding globulin transport protein]] | [[Category: corticosteroid-binding globulin transport protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:45 2008'' |
Revision as of 02:09, 31 March 2008
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| , resolution 1.93Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL
Overview
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.
About 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.
Reference
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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