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| {{STRUCTURE_1m14| PDB=1m14 | SCENE= }} | | {{STRUCTURE_1m14| PDB=1m14 | SCENE= }} |
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| '''Tyrosine Kinase Domain from Epidermal Growth Factor Receptor'''
| | ===Tyrosine Kinase Domain from Epidermal Growth Factor Receptor=== |
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| ==Overview==
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| The crystal structure of the kinase domain from the epidermal growth factor receptor (EGFRK) including forty amino acids from the carboxyl-terminal tail has been determined to 2.6-A resolution, both with and without an EGFRK-specific inhibitor currently in Phase III clinical trials as an anti-cancer agent, erlotinib (OSI-774, CP-358,774, Tarceva(TM)). The EGFR family members are distinguished from all other known receptor tyrosine kinases in possessing constitutive kinase activity without a phosphorylation event within their kinase domains. Despite its lack of phosphorylation, we find that the EGFRK activation loop adopts a conformation similar to that of the phosphorylated active form of the kinase domain from the insulin receptor. Surprisingly, key residues of a putative dimerization motif lying between the EGFRK domain and carboxyl-terminal substrate docking sites are found in close contact with the kinase domain. Significant intermolecular contacts involving the carboxyl-terminal tail are discussed with respect to receptor oligomerization. | | The line below this paragraph, {{ABSTRACT_PUBMED_12196540}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12196540 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12196540}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transferase]] | | [[Category: Transferase]] |
| [[Category: Tyrosine kinase domain]] | | [[Category: Tyrosine kinase domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:30:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:59:19 2008'' |