2v95: Difference between revisions

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[[Image:2v95.gif|left|200px]]
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{{STRUCTURE_2v95|  PDB=2v95  |  SCENE=  }}
'''STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL'''


==Structure of Corticosteroid-Binding Globulin in complex with Cortisol==
<StructureSection load='2v95' size='340' side='right'caption='[[2v95]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2v95]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V95 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCY:(11ALPHA,14BETA)-11,17,21-TRIHYDROXYPREGN-4-ENE-3,20-DIONE'>HCY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v95 OCA], [https://pdbe.org/2v95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v95 RCSB], [https://www.ebi.ac.uk/pdbsum/2v95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v95 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBG_RAT CBG_RAT] Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.<ref>PMID:17644521</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/2v95_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v95 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:17644521</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 2v95" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Corticosteroid-binding globulin|Corticosteroid-binding globulin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Klieber MA]]
[[Category: Klieber, M A.]]
[[Category: Muller YA]]
[[Category: Muller, Y A.]]
[[Category: Cbg]]
[[Category: Corticosteroid-binding globulin transport protein]]
[[Category: Glucocorticoid]]
[[Category: Glycoprotein]]
[[Category: Lipid-binding]]
[[Category: Rcl]]
[[Category: Secreted]]
[[Category: Serpin]]
[[Category: Steroid transporter]]
[[Category: Steroid-binding]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:24:38 2008''

Latest revision as of 15:10, 13 December 2023

Structure of Corticosteroid-Binding Globulin in complex with Cortisol

2v95, resolution 1.93Å

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