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Article

Mutations of neighboring polar residues on the second transmembrane helix disrupt signaling by the parathyroid hormone receptor.

Molecular endocrinology (Baltimore, Md.) - 1 Feb 1996

Turner P R, Bambino T, Nissenson R A

Abstract excerpt

Site-directed mutagenesis was used to assess the role of transmembrane (TM)-charged amino acids in the expression and function of the G protein-coupled receptor for PTH and PTH-related protein (PTHrP). Charged residues that are conserved in the TM regions of most or all members of the PTH/secretin receptor subfamily were targeted. Four mutants (E296A, R337A, H414A, and E459K) displayed properties similar to the...

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Source

Identifiers

PMID: 8825553
DOI: 10.1210/mend.10.2.8825553

Genes

PTH

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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