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1GP0

Human IGF2R domain 11

Summary for 1GP0
Entry DOI10.2210/pdb1gp0/pdb
Related1E6F 1GP3
DescriptorCATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR, SULFATE ION (3 entities in total)
Functional Keywordsreceptor, insulin-like growth factor, cation independent mannose 6-phosphate, transport, beta barrel
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight15660.74
Authors
Brown, J.,Esnouf, R.M.,Jones, M.A.,Linnell, J.,Harlos, K.,Hassan, A.B.,Jones, E.Y. (deposition date: 2001-10-29, release date: 2002-02-28, Last modification date: 2024-11-13)
Primary citationBrown, J.,Esnouf, R.M.,Jones, M.A.,Linnell, J.,Harlos, K.,Hassan, A.B.,Jones, E.Y.
Structure of a Functional Igf2R Fragment Determined from the Anomalous Scattering of Sulfur
Embo J., 21:1054-, 2002
Cited by
PubMed Abstract: 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).
PubMed: 11867533
DOI: 10.1093/EMBOJ/21.5.1054
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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