A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation.

doi:10.1124/mol.54.6.968

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Article

A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation.

Molecular pharmacology - 1 Dec 1998

Colson A O, Perlman J H, Jinsi-Parimoo A, Nussenzveig D R, Osman R, Gershengorn M C

Abstract excerpt

We have studied the role of a highly conserved tryptophan and other aromatic residues of the thyrotropin-releasing hormone (TRH) receptor (TRH-R) that are predicted by computer modeling to form a hydrophobic cluster between transmembrane helix (TM)5 and TM6. The affinity of a mutant TRH-R, in whi...

Topics

Animals
COS Cells
Cell Membrane
Computer Simulation
Luciferases
Midazolam
Models, Molecular
Mutation
Phenylalanine
Plasmids
Protein Conformation
Receptors, Thyrotropin-Releasing Hormone
Transfection
Tryptophan
Tyrosine

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PMID: 9855624
DOI: 10.1124/mol.54.6.968

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9855624-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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