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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 A 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).

Original publication

DOI

10.1093/emboj/21.5.1054

Type

Journal article

Journal

EMBO J

Publication Date

01/03/2002

Volume

21

Pages

1054 - 1062

Keywords

Amino Acid Sequence, Amino Acid Substitution, Animals, Binding Sites, Chickens, Crystallography, X-Ray, Evolution, Molecular, Humans, Insulin-Like Growth Factor II, Mammals, Models, Molecular, Neoplasm Proteins, Point Mutation, Polymorphism, Genetic, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Receptor, IGF Type 2, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Structure-Activity Relationship