| Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur. | |
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MedLine Citation:
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PMID: 11867533 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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). |
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Authors:
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James Brown; Robert M Esnouf; Margaret A Jones; Jane Linnell; Karl Harlos; A Bassim Hassan; E Yvonne Jones |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The EMBO journal Volume: 21 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 2002 Mar |
Date Detail:
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Created Date: 2002-02-27 Completed Date: 2002-05-14 Revised Date: 2013-04-18 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England |
Other Details:
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Languages: eng Pagination: 1054-62 Citation Subset: IM |
Affiliation:
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Cancer Research UK Receptor Structure Research Group, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/1E6F; 1GP0; 1GP3 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acid Substitution Animals Binding Sites Chickens / metabolism Crystallography, X-Ray Evolution, Molecular Humans Insulin-Like Growth Factor II / metabolism Mammals / metabolism Models, Molecular Neoplasm Proteins / genetics Point Mutation Polymorphism, Genetic Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Receptor, IGF Type 2 / chemistry*, genetics, metabolism Sequence Alignment Sequence Homology, Amino Acid Species Specificity Structure-Activity Relationship |
| Chemical | |
Reg. No./Substance:
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0/Neoplasm Proteins; 0/Receptor, IGF Type 2; 67763-97-7/Insulin-Like Growth Factor II |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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