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Article

Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers.

Biochemistry - 2 Oct 2007

You Min, Spangler Jamie, Li Edwin, Han Xue, Ghosh Pijush, Hristova Kalina

Abstract excerpt

Mutations in fibroblast growth factor receptors are known as the genetic basis of skeletal growth disorders. The mechanism of pathogenesis, as determined by mutation-induced changes in receptor structure, interactions, and function, is elusive. Here we study three pathogenic Cys mutations, associated with either thanatophoric dysplasia or achondroplasia, in the TM domain of fibroblast growth factor receptors 3...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17845056
DOI: 10.1021/bi700986n

Genes

FGFR3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers.PMID 17845056Read ↗

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Neutron diffraction studies of fluid bilayers with transmembrane proteins: structural consequences of the achondroplasia mutation.Semantic proximity Read ↗

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