2v95
From Proteopedia
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[[Image:2v95.gif|left|200px]] | [[Image:2v95.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2v95| PDB=2v95 | SCENE= }} | |
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'''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL''' | '''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V95 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry | + | 2V95 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2v6d 2v6d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V95 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Klieber, M A.]] | [[Category: Klieber, M A.]] | ||
[[Category: Muller, Y A.]] | [[Category: Muller, Y A.]] | ||
| - | [[Category: | + | [[Category: Cbg]] |
| - | [[Category: | + | [[Category: Corticosteroid-binding globulin transport protein]] |
| - | [[Category: | + | [[Category: Glucocorticoid]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Lipid-binding]] |
| - | [[Category: | + | [[Category: Rcl]] |
| - | [[Category: | + | [[Category: Secreted]] |
| - | [[Category: | + | [[Category: Serpin]] |
| - | [[Category: | + | [[Category: Steroid transporter]] |
| - | [[Category: | + | [[Category: Steroid-binding]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:24:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:24, 4 May 2008
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 Page seeded by OCA on Sun May 4 18:24:38 2008
