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

Journal article

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).

Authors: Brown, J; Esnouf, R; Jones, M; Linnell, J; Harlos, K

• Publication status: Published
• Journal: EMBO journal
• Volume: 21
• Issue: 5
• Pages: 1054-1062
• Publication date: 2002-03-01
• DOI: 10.1093/emboj/21.5.1054
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Polymorphism, Genetic; Humans; Mammals; Binding Sites; Protein Structure, Tertiary; Models, Molecular; Evolution, Molecular; Receptor, IGF Type 2; Amino Acid Substitution; Species Specificity; Neoplasm Proteins; Chickens; Sequence Alignment; Insulin-Like Growth Factor II; Sequence Homology, Amino Acid; Amino Acid Sequence; Structure-Activity Relationship; Point Mutation; Crystallography, X-Ray; Animals; Protein Conformation; Protein Structure, Secondary