2v95
STRUTURE OF CORTICOSTEROID-BINDING GLOBULIN IN COMPLEX WITH CORTISOL
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OverviewOverview
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 1.9 A crystal structure of rat, CBG shows that its steroid-binding site resembles the thyroxin-binding, site in the related serpin, thyroxin-binding globulin (TBG), and, mutagenesis studies have confirmed the contributions of key residues that, constitute the steroid-binding pocket. Unlike thyroxin-bound TBG, the, cortisol-bound CBG displays an "active" serpin conformation with the, proteinase-sensitive, reactive centre 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, ... [(full description)]
About this StructureAbout this Structure
2V95 is a [Single protein] structure of sequence from [Rattus norvegicus] with PDN as [ligand]. This structure superseeds the now removed PDB entry 2V6D. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Corticosteroid-binding globulin: structural basis for steroid transport and proteinase-triggered release., Klieber MA, Underhill C, Hammond GL, Muller YA, J Biol Chem. 2007 Jul 19;. PMID:17644521
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