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| {{STRUCTURE_2gs6| PDB=2gs6 | SCENE= }} | | {{STRUCTURE_2gs6| PDB=2gs6 | SCENE= }} |
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| '''Crystal Structure of the active EGFR kinase domain in complex with an ATP analog-peptide conjugate'''
| | ===Crystal Structure of the active EGFR kinase domain in complex with an ATP analog-peptide conjugate=== |
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| ==Overview==
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| The mechanism by which the epidermal growth factor receptor (EGFR) is activated upon dimerization has eluded definition. We find that the EGFR kinase domain can be activated by increasing its local concentration or by mutating a leucine (L834R) in the activation loop, the phosphorylation of which is not required for activation. This suggests that the kinase domain is intrinsically autoinhibited, and an intermolecular interaction promotes its activation. Using further mutational analysis and crystallography we demonstrate that the autoinhibited conformation of the EGFR kinase domain resembles that of Src and cyclin-dependent kinases (CDKs). EGFR activation results from the formation of an asymmetric dimer in which the C-terminal lobe of one kinase domain plays a role analogous to that of cyclin in activated CDK/cyclin complexes. The CDK/cyclin-like complex formed by two kinase domains thus explains the activation of EGFR-family receptors by homo- or heterodimerization. | | The line below this paragraph, {{ABSTRACT_PUBMED_16777603}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16777603 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16777603}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Egfr]] | | [[Category: Egfr]] |
| [[Category: Kinase,active]] | | [[Category: Kinase,active]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:27:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:07:15 2008'' |