2ceo | pdb_00002ceo
THYROXINE-BINDING GLOBULIN COMPLEX WITH THYROXINE
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Overview
The hormones that most directly control tissue activities in health and, disease are delivered by two noninhibitory members of the serpin family of, protease inhibitors, thyroxine-binding globulin (TBG) and, corticosteroid-binding globulin. The structure of TBG bound to tetra-iodo, thyroxine, solved here at 2.8 A, shows how the thyroxine is carried in a, surface pocket on the molecule. This unexpected binding site is confirmed, by mutations associated with a loss of hormone binding in both TBG and, also homologously in corticosteroid-binding globulin. TBG strikingly, differs from other serpins in having the upper half of its main beta-sheet, fully opened, so its reactive center peptide loop can readily move in and, out of the sheet to give an equilibrated binding and release of ... [(full description)]
About this Structure
2CEO is a [Single protein] structure of sequence from [Homo sapiens] with T44 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural mechanism for the carriage and release of thyroxine in the blood., Zhou A, Wei Z, Read RJ, Carrell RW, Proc Natl Acad Sci U S A. 2006 Sep 5;103(36):13321-6. Epub 2006 Aug 28. PMID:16938877
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