Corticosteroid-binding globulin: Difference between revisions
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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>. | ||
In its native form, CBG is in the "stressed" conformation and binds cortisol with very high affinity.<Structure load='2V95' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | 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='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> Upon cleavage by its target proteinase, believed to be human neutrophil elastase, the entire N-terminal segment of the reactive loop is inserted into beta-sheet A where it is incorporated as a novel beta-strand. This causes rearrangements in the main chain ast serveral parts of the serpin fold, resulting in what is conventionally known as the "relaxed" state <ref>PMID:18513745 </ref>,<ref>PMID:3143075 </ref>. | ||
