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1igl
From Proteopedia
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SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS
Contents |
Overview
The three-dimensional structure of human insulin-like growth factor (IGF), II in aqueous solution at pH 3.1 and 300 K has been determined from, nuclear magnetic resonance data and restrained molecular dynamics, calculations. Structural constraints consisting of 502 NOE-derived, distance constraints, 11 dihedral angle restraints, and three disulfide, bridges were used as input for distance geometry calculations in DIANA and, X-PLOR, followed by simulated annealing refinement and energy minimization, in X-PLOR. The resulting family of 20 structures was well defined in the, regions of residues 5 to 28 and 41 to 62, with an average pairwise, root-mean-square deviation of 1.24 A for the backbone heavy-atoms (N, C2, C) and 1.90 A for all heavy atoms. The poorly defined regions consist of, the N and C termini, part of the B-domain, and the C-domain loop., Resonances from these regions of the protein gave stronger cross peaks in, two dimensional NMR spectra, consistent with significant motional, averaging. The main secondary structure elements in IGF-II are, alpha-helices encompassing residues 11 to 21, 42 to 49 and 53 to 59. A, small anti-parallel beta-sheet is formed by residues 59 to 61 and 25 to, 27, while residues 26 to 28 appear to participate in intermolecular, beta-sheet formation. The structure of IGF-II in the well-defined regions, is very similar to those of the corresponding regions of insulin and, IGF-I. Significant differences between IGF-II and IGF-I occur near the, start of the third helix, in a region known to modulate affinity for the, type 2 IGF receptor, and at the C terminus. The IGF II structure is, discussed in relation to its binding sites for the insulin and IGF, receptors and the IGF binding proteins.
Disease
Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[147470]
About this Structure
1IGL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions., Torres AM, Forbes BE, Aplin SE, Wallace JC, Francis GL, Norton RS, J Mol Biol. 1995 Apr 28;248(2):385-401. PMID:7739048
Page seeded by OCA on Mon Nov 12 17:29:39 2007
