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  • The EMBO Journal (2002) 21, 1054 - 1062
  • doi:10.1093/emboj/21.5.1054

Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur

James Brown1, Robert M. Esnouf1, Margaret A. Jones1, Jane Linnell2, Karl Harlos1, A.Bassim Hassan2 and E.Yvonne Jones2

  1. Cancer Research UK Receptor Structure Research Group, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK
  2. Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK

Correspondence to:

E.Yvonne Jones, E-mail: Yvonne.Jones@strubi.ox.ac.uk

Received 15 November 2001; Accepted 10 January 2002; Revised 28 December 2001

Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind IGF-II. IGF2R contains 15 homologous extracellular domains, with domain 11 primarily responsible for IGF-II binding. We report a 1.4 Å resolution crystal structure of domain 11, solved using the anomalous scattering signal of sulfur. The structure consists of two crossed beta-sheets forming a flattened beta-barrel. Structural analysis identifies the putative IGF-II binding site at one end of the beta-barrel whilst crystal lattice contacts suggest a model for the full-length IGF2R extracellular region. The structure factors and coordinates of IGF2R domain 11 have been deposited in the Protein Data Bank (accession codes 1GP0 and 1GP3).

  • Keywords:

    • growth factor receptor,
    • IGF-II,
    • protein crystallography,
    • tumour suppression