Growth factor receptor cysteine-rich domain superfamily (IPR009030)
Short name: Growth_fac_rcpt_cys_sf
- Insulin-like growth factor-binding protein, IGFBP (IPR000867)
- Furin-like cysteine-rich domain (IPR006211)
- Notch (IPR008297)
- Insulin-like growth factor binding protein-related protein (IGFBP-rP), MAC25 (IPR011390)
- IGFBP-related, CNN (IPR012395)
- Tyrosine protein kinase, EGF/ERB/XmrK receptor (IPR016245)
- Tyrosine-protein kinase, insulin-like receptor (IPR016246)
- Pro-epidermal growth factor (IPR016317)
- Insulin-like growth factor-binding protein family 1-6, chordata (IPR022321)
- Insulin-like growth factor-binding protein 1 (IPR022322)
- Insulin-like growth factor-binding protein 6 (IPR022326)
- Insulin-like growth factor-binding protein 4 (IPR022327)
- Neurogenic locus Notch 2 (IPR022336)
- Matrilin-2 (IPR030747)
- Epidermal growth factor-like protein 6 (IPR032930)
- Fibulin 3/4/5 (IPR037287)
- Fibulin-5 (IPR037288)
- Endothelial cell-specific molecule 1 (IPR038850)
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 beta-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.
ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. The extracellular region of ErbB3 is made up of two Cys-rich domains and two L-domains, arranged alternately [PMID: 12154198]. The two L-domains and the first Cys-rich domain are structurally homologous to those found in IGF-1R. The two Cys-rich domains are extended repeats of seven small disulphide-containing modules. A beta-hairpin loop extends from the first Cys-rich domain to contact the C-terminal portion of the second Cys-rich domain, creating a large pore structure.
- SSF57184 (SSF57184)