2v95

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[[Image:2v95.gif|left|200px]]<br /><applet load="2v95" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2v95.gif|left|200px]]
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caption="2v95, resolution 1.93&Aring;" />
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'''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL'''<br />
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{{Structure
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|PDB= 2v95 |SIZE=350|CAPTION= <scene name='initialview01'>2v95</scene>, resolution 1.93&Aring;
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|SITE= <scene name='pdbsite=AC1:Pdn+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PDN:17,21-DIHYDROXYPREGNA-1,4-DIENE-3,11,20-TRIONE'>PDN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2V95 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=PDN:'>PDN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 2V6D. Known structural/functional Site: <scene name='pdbsite=AC1:Pdn+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V95 OCA].
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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 2V6D. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V95 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17644521 17644521]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17644521 17644521]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: cbg]]
[[Category: cbg]]
[[Category: corticosteroid-binding globulin transport protein]]
[[Category: corticosteroid-binding globulin transport protein]]
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[[Category: glucocorticoids]]
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[[Category: glucocorticoid]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
[[Category: lipid-binding]]
[[Category: lipid-binding]]
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:44:24 2008''

Revision as of 16:44, 20 March 2008


PDB ID 2v95

Drag the structure with the mouse to rotate
, resolution 1.93Å
Sites:
Ligands:
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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