1igr
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TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)
OverviewOverview
The type-1 insulin-like growth-factor receptor (IGF-1R) and insulin, receptor (IR) are closely related members of the tyrosine-kinase receptor, superfamily. IR is essential for glucose homeostasis, whereas IGF-1R is, involved in both normal growth and development and malignant, transformation. Homologues of these receptors are found in animals as, simple as cnidarians. The epidermal growth-factor receptor (EGFR) family, is closely related to the IR family and has significant sequence identity, to the extracellular portion we describe here. We now present the, structure of the first three domains of IGF-IR (L1-Cys-rich-L2) determined, to 2.6 A resolution. The L domains each consist of a single-stranded, right-handed beta-helix. The Cys-rich region is composed of eight, disulphide-bonded modules, seven of which form a rod-shaped domain with, modules associated in an unusual manner. The three domains surround a, central space of sufficient size to accommodate a ligand molecule., Although the fragment (residues 1-462) does not bind ligand, many of the, determinants responsible for hormone binding and ligand specificity map to, this central site. This structure therefore shows how the IR subfamily, might interact with their ligands.
DiseaseDisease
Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[147370]
About this StructureAbout this Structure
1IGR is a Single protein structure of sequence from Homo sapiens with NAG and SO4 as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor., Garrett TP, McKern NM, Lou M, Frenkel MJ, Bentley JD, Lovrecz GO, Elleman TC, Cosgrove LJ, Ward CW, Nature. 1998 Jul 23;394(6691):395-9. PMID:9690478
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