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spinqualitylabelsall models 1imx, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

1.8 Angstrom crystal structure of IGF-1

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Despite efforts spanning considerably more than a decade, a, high-resolution view of the family of proteins known as insulin-like, growth factors (IGFs) has remained elusive. IGF-1 consists of three, helical segments which are connected by a 12-residue linker known as the, C-region. NMR studies of members of this family reveal a dynamic structure, with a topology resembling insulin but little structural definition in the, C-region. We have crystallized IGF-1 in the presence of the detergent, deoxy big CHAPS, and determined its structure at 1.8 A resolution by, multiwavelength anomalous diffraction, exploiting the anomalous scattering, of a single bromide ion and six of the seven sulfur atoms of IGF-1. The, structure reveals a well-defined conformation for much of the C-region, which extends away from the core of IGF-1 and has residues known to be, involved in receptor binding prominently displayed in a type II beta-turn., In the crystal, these residues form a dimer interface, but analytical, ultracentrifugation experiments demonstrate that at physiological, concentrations IGF-1 is monomeric. A single detergent molecule contacts, residues known to be important for IGF-1 binding protein (IGFBP), interactions. Biophysical and biochemical data show that the detergent, binds to IGF-1 specifically and blocks binding of IGFBP-1 and IGFBP-3.

Disease

Known disease associated with this structure: Growth retardation with deafness and mental retardation due to IGF1 deficiency OMIM:[147440]

About this Structure

1IMX is a Single protein structure of sequence from Homo sapiens with BR and CPQ as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions., Vajdos FF, Ultsch M, Schaffer ML, Deshayes KD, Liu J, Skelton NJ, de Vos AM, Biochemistry. 2001 Sep 18;40(37):11022-9. PMID:11551198

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