Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding.

doi:10.1242/jcs.03036

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Article

Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding.

Journal of cell science - 1 Aug 2006

van den Eijnden Monique J M, Lahaye Liza L, Strous Ger J

Abstract excerpt

The growth hormone receptor contains seven cysteine residues in its extracellular domain. The six in the growth hormone binding domain form disulfide bonds, and help the receptor to gain its correct three-dimensional structure. In this study we replaced the cysteine for serine and alanine residues and investigated their role in growth hormone receptor folding, dimerisation and signal transduction. Folding and...

Topics

Animals
Dimerization
Disulfides
Ligands
Models, Molecular
Mutation
Protein Conformation
Protein Folding
Rabbits
Receptors, Somatotropin
Signal Transduction

Source

Open in PubMed

Identifiers

PMID: 16820415
DOI: 10.1242/jcs.03036

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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