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'' | ||