期刊
ANNUAL REVIEW OF BIOPHYSICS
卷 37, 期 -, 页码 353-373出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.37.032807.125829
关键词
EGFR; ligand-induced receptor dimerization; mechanisms of activation and inhibition; receptor tyrosine kinase
类别
资金
- NCI NIH HHS [R01 CA112552-04, R01 CA112552] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA112552] Funding Source: NIH RePORTER
High-resolution X-ray crystal structures determined in the past six years dramatically influence our view of ligand-induced activation of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. Ligand binding to the extracellular region of EGFR promotesa major domain reorganization, plus local conformational changes, that are required to generate an entirely receptor-mediated dimer. In this activated complex the intracellular kinase domains associate to form on asymmetric dimer that supports the allosteric activation of one kinase. These models are discussed with emphasis on recent studies that add details or bolster the generality of this view of activation of this family of receptors. The EGFR family is implicated in several disease states, perhaps most notably in cancers. Activating tumor mutations have been identified in the intracellular and extracellular regions of EGFR. The impact of these tumor mutations on the understanding of EGFR activation and of its inhibition is discussed.
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