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Article

FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.

Biophysical journal - 2 Jul 2013

Sarabipour Sarvenaz, Hristova Kalina

Abstract excerpt

Isolated receptor tyrosine kinase transmembrane (TM) domains have been shown to form sequence-specific dimers in membranes. Yet, it is not clear whether studies of isolated TM domains yield knowledge that is relevant to full-length receptors or whether the large glycosylated extracellular domains alter the interactions between the TM helices. Here, we address this question by quantifying the effect of the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 23823235
DOI: 10.1016/j.bpj.2013.05.053
PMCID: PMC3699758

Genes

FGFR3

Provenance

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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