1gp0: Difference between revisions
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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> | |||
}} | }} | ||
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==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). | ||
==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: 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'' | ||
