Corticosteroid-binding globulin

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<StructureSection load='2V95' size='450' side='right' scene='' caption='Cartoon representation of corticosteroid-binding globulin complex with cortisol, [[2v95]]'>
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[[Image:2v95.png|left|200px|thumb|Crystal Structure of corticosteroid-binding globulin complex with cortisol, [[2v95]]]]
[[Image:2v95.png|left|200px|thumb|Crystal Structure of corticosteroid-binding globulin complex with cortisol, [[2v95]]]]
==Introduction==
==Introduction==
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Previously-solved structures of the human CBG-antitrypsin (Pittsburgh) chimera with cleaved reactive centre loop at 1.84Å and the native rat CBG at 1.9Å confirm that corticosteroid-binding globulin, despite being a non-inhibitory member of the serpin family, undergoes the S-to-R transition just like the inhibitory members <ref>PMID:17644521 </ref>,<ref>PMID:18513745 </ref>.
Previously-solved structures of the human CBG-antitrypsin (Pittsburgh) chimera with cleaved reactive centre loop at 1.84Å and the native rat CBG at 1.9Å confirm that corticosteroid-binding globulin, despite being a non-inhibitory member of the serpin family, undergoes the S-to-R transition just like the inhibitory members <ref>PMID:17644521 </ref>,<ref>PMID:18513745 </ref>.
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In its native form, CBG is in the "stressed" conformation and binds cortisol with very high affinity<ref>PMID:17644521 </ref>.<Structure load='2V95' size='400' frame='true' align='right' caption='Cartoon representation of corticosteroid-binding globulin complex with cortisol, [[2v95]]' scene='Insert optional scene name here' /> Upon cleavage by its target proteinase, believed to be human neutrophil elastase, the protein undergoes structural rearrangements in the main chain at several parts of the serpin fold, resulting in what is conventionally known as the "relaxed" state <ref>PMID:18513745 </ref>,<ref>PMID:3143075 </ref>, as seen <scene name='Corticosteroid-binding_globulin/Cleaved/9'>here</scene>. The main conformational change is the insertion of the entire N-terminal segment of the reactive loop into beta-sheet A where it is incorporated as a <scene name='Corticosteroid-binding_globulin/Cleaved/10'>novel beta-strand</scene>.
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In its native form, CBG is in the "stressed" conformation and binds cortisol with very high affinity<ref>PMID:17644521 </ref>.
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Upon cleavage by its target proteinase, believed to be human neutrophil elastase, the protein undergoes structural rearrangements in the main chain at several parts of the serpin fold, resulting in what is conventionally known as the "relaxed" state <ref>PMID:18513745 </ref>,<ref>PMID:3143075 </ref>, as seen <scene name='Corticosteroid-binding_globulin/Cleaved/9'>here</scene>. The main conformational change is the insertion of the entire N-terminal segment of the reactive loop into beta-sheet A where it is incorporated as a <scene name='Corticosteroid-binding_globulin/Cleaved/10'>novel beta-strand</scene>.
''(Click'' <scene name='Corticosteroid-binding_globulin/Native/1'>here</scene> ''to return to structure of CBG in the S-state.)
''(Click'' <scene name='Corticosteroid-binding_globulin/Native/1'>here</scene> ''to return to structure of CBG in the S-state.)

Revision as of 13:00, 9 June 2015

Cartoon representation of corticosteroid-binding globulin complex with cortisol, 2v95

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Proteopedia Page Contributors and Editors (what is this?)

Wee Lee Chan, Michal Harel, Alexander Berchansky

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