Document Detail


Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur.
MedLine Citation:
PMID:  11867533     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
James Brown; Robert M Esnouf; Margaret A Jones; Jane Linnell; Karl Harlos; A Bassim Hassan; E Yvonne Jones
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The EMBO journal     Volume:  21     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2002 Mar 
Date Detail:
Created Date:  2002-02-27     Completed Date:  2002-05-14     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1054-62     Citation Subset:  IM    
Affiliation:
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.:
PDB/1E6F;  1GP0;  1GP3
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MeSH Terms
Descriptor/Qualifier:
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:
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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