2gs7: Difference between revisions

Revision as of 16:08, 27 July 2008

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File:2gs7.png

Template:STRUCTURE 2gs7

Crystal Structure of the inactive EGFR kinase domain in complex with AMP-PNPCrystal Structure of the inactive EGFR kinase domain in complex with AMP-PNP

Template:ABSTRACT PUBMED 16777603

About this StructureAbout this Structure

2GS7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor., Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J, Cell. 2006 Jun 16;125(6):1137-49. PMID:16777603

Page seeded by OCA on Sun Jul 27 16:08:52 2008

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OCA

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-'''Crystal Structure of the inactive EGFR kinase domain in complex with AMP-PNP'''
+===Crystal Structure of the inactive EGFR kinase domain in complex with AMP-PNP===
-==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
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 ==About this Structure==
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 [[Category: Inactive]]
 [[Category: Kinase]]
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