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Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
Author(s) -
Brown James,
Esnouf Robert M.,
Jones Margaret A.,
Linnell Jane,
Harlos Karl,
Hassan A.Bassim,
Jones E.Yvonne
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.5.1054
Subject(s) - biology , extracellular , insulin like growth factor 2 receptor , biophysics , receptor , crystallography , biochemistry , microbiology and biotechnology , growth factor , insulin like growth factor 1 receptor , chemistry
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 β‐sheets forming a flattened β‐barrel. Structural analysis identifies the putative IGF‐II binding site at one end of the β‐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 ).