Seroatlas · Protein domains

Growth factor receptor cysteine-rich domain superfamily

IPR009030

Definition

This growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) PMID:11447105, the type-1 insulin-like growth-factor receptor (IGF-1R) PMID:9690478, and members of the epidermal growth factor (EGF) receptor family PMID:7567962, such as the receptor protein-tyrosine kinase Erbb-3 (ErbB3) PMID:12154198. The general structure of the growth factor receptor domain is a disulphide-bound fold containing a β-hairpin with two adjacent disulphides. IGFBPs control the distribution, function and activity of insulin-like growth factors (IGFs) IGF-I and IGF-II, which are key regulators of cell proliferation, differentiation and transformation. All IGFBPs share a common domain organisation, where the highest conservation is found in the N-terminal Cys-rich IGF-binding domain. The N-terminal domain contains 10-12 conserved cysteine residues. IGF-1R is a member of the tyrosine-kinase receptor superfamily that is involved in both normal growth and development and malignant transformation. The Cys-rich domain is flanked by two L-domains, and together they contribute to hormone binding and ligand specificity, even though they do not bind ligand directly. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain.

127 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (127 proteins: gene, accession, name)

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