Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
AUTOR(ES)
Brown, James
FONTE
Oxford University Press
RESUMO
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).
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125895Documentos Relacionados
- Dinucleotide repeat polymorphism at the IGF2R locus
- Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.
- Bidirectional action of the Igf2r imprint control element on upstream and downstream imprinted genes
- Imprinted silencing of Slc22a2 and Slc22a3 does not need transcriptional overlap between Igf2r and Air
- Long-range DNase I hypersensitivity mapping reveals the imprinted Igf2r and Air promoters share cis-regulatory elements
