|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
2002-2-27
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
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:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10079240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10089341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10089360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10320398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10446221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10480921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10485478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10514470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10706126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10734317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10764761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10882106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-10892645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-11081635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-11297550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-11438990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-11447105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-11585807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-1323236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-1846448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-2963003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-2963004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-3892003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-537059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-7527339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-7568213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-7797478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-7984417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-8449908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-8691094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-8745398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-8776724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-8811191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-9604938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-9605330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-9817593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11867533-9873065
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0261-4189
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
21
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1054-62
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:11867533-Amino Acid Sequence,
pubmed-meshheading:11867533-Amino Acid Substitution,
pubmed-meshheading:11867533-Animals,
pubmed-meshheading:11867533-Binding Sites,
pubmed-meshheading:11867533-Chickens,
pubmed-meshheading:11867533-Crystallography, X-Ray,
pubmed-meshheading:11867533-Evolution, Molecular,
pubmed-meshheading:11867533-Humans,
pubmed-meshheading:11867533-Insulin-Like Growth Factor II,
pubmed-meshheading:11867533-Mammals,
pubmed-meshheading:11867533-Models, Molecular,
pubmed-meshheading:11867533-Neoplasm Proteins,
pubmed-meshheading:11867533-Point Mutation,
pubmed-meshheading:11867533-Polymorphism, Genetic,
pubmed-meshheading:11867533-Protein Conformation,
pubmed-meshheading:11867533-Protein Structure, Secondary,
pubmed-meshheading:11867533-Protein Structure, Tertiary,
pubmed-meshheading:11867533-Receptor, IGF Type 2,
pubmed-meshheading:11867533-Sequence Alignment,
pubmed-meshheading:11867533-Sequence Homology, Amino Acid,
pubmed-meshheading:11867533-Species Specificity,
pubmed-meshheading:11867533-Structure-Activity Relationship
|
|
pubmed:year |
2002
|
