1wqj

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Revision as of 17:46, 12 November 2007

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spinqualitylabelsall models 1wqj, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structural Basis for the Regulation of Insulin-Like Growth Factors (IGFs) by IGF Binding Proteins (IGFBPs)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Insulin-like growth factor binding proteins (IGFBPs) control the, extracellular distribution, function, and activity of IGFs. Here, we, report an X-ray structure of the binary complex of IGF-I and the, N-terminal domain of IGFBP-4 (NBP-4, residues 3-82) and a model of the, ternary complex of IGF-I, NBP-4, and the C-terminal domain (CBP-4, residues 151-232) derived from diffraction data with weak definition of, the C-terminal domain. These structures show how the IGFBPs regulate IGF, signaling. Key features of the structures include (1) a disulphide bond, ladder that binds to IGF and partially masks the IGF residues responsible, for type 1 IGF receptor (IGF-IR) binding, (2) the high-affinity IGF-I, interaction site formed by residues 39-82 in a globular fold, and (3), CBP-4 interactions. Although CBP-4 does not bind individually to either, IGF-I or NBP-4, in the ternary complex, CBP-4 contacts both and also, blocks the IGF-IR binding region of IGF-I.

Disease

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

About this Structure

1WQJ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the regulation of insulin-like growth factors by IGF binding proteins., Siwanowicz I, Popowicz GM, Wisniewska M, Huber R, Kuenkele KP, Lang K, Engh RA, Holak TA, Structure. 2005 Jan;13(1):155-67. PMID:15642270

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