1irk: Difference between revisions
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[[Image:1irk.gif|left|200px]] | [[Image:1irk.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR''' | {{Structure | ||
|PDB= 1irk |SIZE=350|CAPTION= <scene name='initialview01'>1irk</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=EMC:ETHYL MERCURY ION'>EMC</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IRK is a [ | 1IRK 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=1IRK OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the tyrosine kinase domain of the human insulin receptor., Hubbard SR, Wei L, Ellis L, Hendrickson WA, Nature. 1994 Dec 22-29;372(6508):746-54. PMID:[http:// | Crystal structure of the tyrosine kinase domain of the human insulin receptor., Hubbard SR, Wei L, Ellis L, Hendrickson WA, Nature. 1994 Dec 22-29;372(6508):746-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7997262 7997262] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase (phosphotransferase)]] | [[Category: transferase (phosphotransferase)]] | ||
''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 11:53:59 2008'' | ||
Revision as of 12:54, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR
OverviewOverview
The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.
DiseaseDisease
Known diseases associated with this structure: Diabetes mellitus, insulin-resistant, with acanthosis nigricans OMIM:[147670], Hyperinsulinemic hypoglycemia, familial, 5 OMIM:[147670], Leprechaunism OMIM:[147670], Rabson-Mendenhall syndrome OMIM:[147670]
About this StructureAbout this Structure
1IRK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the tyrosine kinase domain of the human insulin receptor., Hubbard SR, Wei L, Ellis L, Hendrickson WA, Nature. 1994 Dec 22-29;372(6508):746-54. PMID:7997262
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