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Article

Intramolecular disulfide bonds of the prolactin receptor short form are required for its inhibitory action on the function of the long form of the receptor.

Molecular and cellular biology - 1 May 2009

Xie Y-L, Hassan S A, Qazi A M, Tsai-Morris C H, Dufau M L

Abstract excerpt

The short form (S1b) of the prolactin receptor (PRLR) silences prolactin-induced activation of gene transcription by the PRLR long form (LF). The functional and structural contributions of two intramolecular disulfide (S-S) bonds within the extracellular subdomain 1 (D1) of S1b to its inhibitory function on the LF were investigated. Mutagenesis of the paired cysteines eliminated the inhibitory action of S1b. The...

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Cysteine
Dimerization
Disulfides
Genes, Reporter
Janus Kinase 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Multimerization

Receptors, Prolactin

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Open in PubMed Open full text

Identifiers

PMID: 19273600
DOI: 10.1128/MCB.01716-08
PMCID: PMC2682051

Genes

PRLR
JAK2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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