1gp0: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1gp0.gif|left|200px]] | [[Image:1gp0.gif|left|200px]] | ||
'''HUMAN IGF2R DOMAIN 11''' | {{Structure | ||
|PDB= 1gp0 |SIZE=350|CAPTION= <scene name='initialview01'>1gp0</scene>, resolution 1.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HUMAN IGF2R DOMAIN 11''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1GP0 is a [ | 1GP0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP0 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11867533 11867533] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 30: | Line 39: | ||
[[Category: transport]] | [[Category: transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:03 2008'' | ||
Revision as of 12:26, 20 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN IGF2R DOMAIN 11
OverviewOverview
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).
DiseaseDisease
Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[147280]
About this StructureAbout this Structure
1GP0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Mar 20 11:26:03 2008