Corticosteroid-binding globulin: Difference between revisions

Revision as of 20:46, 7 June 2012 view source Wee Lee Chan (talk \| contribs) 40 edits No edit summary ← Older edit		Revision as of 20:47, 7 June 2012 view source Wee Lee Chan (talk \| contribs) 40 edits No edit summary Newer edit →
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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.		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' />

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