1gp0
From Proteopedia
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| |PDB= 1gp0 |SIZE=350|CAPTION= <scene name='initialview01'>1gp0</scene>, resolution 1.40Å | |PDB= 1gp0 |SIZE=350|CAPTION= <scene name='initialview01'>1gp0</scene>, resolution 1.40Å | ||
| |SITE=  | |SITE=  | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | 
| |ACTIVITY=  | |ACTIVITY=  | ||
| |GENE=  | |GENE=  | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp0 OCA], [http://www.ebi.ac.uk/pdbsum/1gp0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gp0 RCSB]</span> | ||
| }} | }} | ||
| Line 14: | Line 17: | ||
| ==Overview== | ==Overview== | ||
| 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). | 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). | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147280 147280]] | ||
| ==About this Structure== | ==About this Structure== | ||
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| [[Category: Jones, M A.]] | [[Category: Jones, M A.]] | ||
| [[Category: Linnell, J.]] | [[Category: Linnell, J.]] | ||
| - | [[Category: SO4]] | ||
| [[Category: beta barrel]] | [[Category: beta barrel]] | ||
| [[Category: cation independent mannose 6-phosphate]] | [[Category: cation independent mannose 6-phosphate]] | ||
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| [[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:29 2008'' | 
Revision as of 17:48, 30 March 2008
 
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| , resolution 1.40Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN IGF2R DOMAIN 11
Overview
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).
About this Structure
1GP0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur., Brown J, Esnouf RM, Jones MA, Linnell J, Harlos K, Hassan AB, Jones EY, EMBO J. 2002 Mar 1;21(5):1054-62. PMID:11867533
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