Crystal structure of the thyroid hormone receptor beta ligand binding domain in complex with a beta selective compound

File:1r6g.gif


1r6g, resolution 3.00Å

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OverviewOverview

A set of thyromimetics having improved selectivity for TR-beta1 were prepared by replacing the 3'-isopropyl group of 2 and 3 with substituents having increased steric bulk. From this limited SAR study, the most potent and selective compounds identified were derived from 2 and contained a 3'-phenyl moiety bearing small hydrophobic groups meta to the biphenyl link. X-ray crystal data of 15c complexed with TR-beta1 LBD shows methionine 442 to be displaced by the bulky R3' phenyl ethyl amide side chain. Movement of this amino acid side chain provides an expanded pocket for the bulky side chain while the ligand-receptor complex retains full agonist activity.

DiseaseDisease

Known diseases associated with this structure: Thyroid hormone resistance OMIM:[190160], Thyroid hormone resistance, autosomal recessive OMIM:[190160]

About this StructureAbout this Structure

1R6G is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Thyroid receptor ligands. Part 2: Thyromimetics with improved selectivity for the thyroid hormone receptor beta., Hangeland JJ, Doweyko AM, Dejneka T, Friends TJ, Devasthale P, Mellstrom K, Sandberg J, Grynfarb M, Sack JS, Einspahr H, Farnegardh M, Husman B, Ljunggren J, Koehler K, Sheppard C, Malm J, Ryono DE, Bioorg Med Chem Lett. 2004 Jul 5;14(13):3549-53. PMID:15177471

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