1irk: Difference between revisions
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|PDB= 1irk |SIZE=350|CAPTION= <scene name='initialview01'>1irk</scene>, resolution 2.1Å | |PDB= 1irk |SIZE=350|CAPTION= <scene name='initialview01'>1irk</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=EMC:ETHYL MERCURY ION'>EMC</scene> | |LIGAND= <scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1irk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irk OCA], [http://www.ebi.ac.uk/pdbsum/1irk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1irk RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Hubbard, S R.]] | [[Category: Hubbard, S R.]] | ||
[[Category: Wei, L.]] | [[Category: Wei, L.]] | ||
[[Category: transferase (phosphotransferase)]] | [[Category: transferase (phosphotransferase)]] | ||
''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 21:23:37 2008'' | ||
Revision as of 18:23, 30 March 2008
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| 1irk, resolution 2.1Å | |||||||||||||
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| Ligands: | EMC | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR
Overview
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.
About this Structure
1IRK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
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:7997262
Page seeded by OCA on Sun Mar 30 21:23:37 2008
