An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.

By Xuewu Zhang, Jodi Gureasko, Kui Shen, P. Cole, J. Kuriyan. Cell, 2006

1,611 citations recorded by the source corpus.

Subfields: Genetics, Oncology, Pulmonary and Respiratory Medicine

View Paper: https://www.semanticscholar.org/paper/f15d8d817671d6887618ecc2687c3dea2dc067d6

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In Genetics

1. Ping Wee
2. Zhixiang Wang
3. D. Ron
4. R. Roskoski

In Oncology

1. R. Roskoski
2. M. Moasser
3. Ping Wee
4. Zhixiang Wang
5. J. Baselga
6. P. Jänne
7. Yigong Shi
8. S. Swain

In Pulmonary and Respiratory Medicine

1. P. Jänne
2. J. Baselga
3. R. Roskoski
4. J. Engelman
5. Jin-Yuan Shih
6. Shang-Gin Wu

Citations in the corpus

• Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment (2009, neutral): “…with the transmembrane domain dimer and couples to the asymmetric kinase domain dimer via the dimeric JM-A helices and the juxtamembrane latch. conformation as in our structure, but do not show extensive contacts within symmetrical dimers (Wood et al., 2004; Xu et al., 2008; Zhang et al., 2006).”
• Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. (2007, background): “Additionally, while the present work was in review, Zhang et al. reported an 20-fold (kcat/Km) activation of the L858R mutant kinase in vitro (Zhang et al., 2006), and in a separate study Carey et al. found an 2-fold increase in its Km for ATP (Carey et al., 2006).”
• The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “The kinase domain of EGFR generally exists in an auto-inhibited inactive conformation that adopts an active conformation by asymmetric contacts made during receptor dimerization [36].”
• HSP90 at the hub of protein homeostasis: emerging mechanistic insights (2010, background): “A mutation in EGFR (Leu858Arg) constitutively activates the receptor by destabilizing its inactive conformatio”
• Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “The EGFR dimer is an asymmetric EGFR dimer pair, in that the C-terminus of the activating kinase inserts into the active site of the receiving kinase, so that this allosteric interaction can activate the receiving kinase, resulting in transautophosphorylation [72].”
• A glimpse of structural biology through X-ray crystallography. (2014, background): “The activation mechanism of EGFR has been elegantly revealed by crystallographic discovery and subsequent biochemical analysis (Burgess et al., 2003; Zhang et al., 2006).”
• GC1118, an Anti-EGFR Antibody with a Distinct Binding Epitope and Superior Inhibitory Activity against High-Affinity EGFR Ligands (2015, background): “6 Structural studies of the EGF-EGFR complex depict the process of EGFR activation after ligand binding (19-22), which triggers a conformational change in EGFR from a tethered form to an open form.”
• Mechanisms of receptor tyrosine kinase activation in cancer (2018, neutral): “of an asymmetric dimer between two receptor molecules [9].”
• The Arabidopsis NPR1 protein is a receptor for the plant defense hormone salicylic acid. (2012, background): “The conformation of RLK changes upon ligand binding, which allows for the autophosphorylation of the kinase domain (Zhang et al., 2006a), and/or the phosphorylation of downstream signaling components that interact with the kinase domain (Wang et al., 2008).”
• Mechanism of activation and inhibition of the HER4/ErbB4 kinase. (2008, methodology): “Discovery of the importance of an asymmetric EGFR kinase dimer for regulation of kinase activity provided a satisfying link between ligand-induced receptor dimerization and kinase activation (Burgess et al., 2003; Jeffrey et al., 1995; Zhang et al., 2006).”
• Emerging functions of the EGFR in cancer (2017, background): “Ligand binding promotes receptor dimerization, which determines a series of structural rearrangements that are conveyed to the cytoplasmic domain allowing the formation of asymmetric dimers between the two juxtaposed catalytic domains (Zhang et al., 2006; Fig.”
• Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains (2013, methodology): “5A) was bound to liposomes containing 1% lipid with a nickel-nitrilotriacetic acid (NTA)–bearing head group (28).”
• Activity profiles of 309 ToxCast™ chemicals evaluated across 292 biochemical targets. (2011, background): “Purified recombinant kinase may, however, require allosteric echanisms and aggregation to release the tyrosine kinase domain rom autoinhibition (Zhang et al., 2006).”
• Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker (2012, background): “342 at A SPE T Journals on D ecem ber 19, 2018 jpet.aspetjournals.org D ow nloaded from activator and induces activation of the intrinsic catalytic activity of the partnered receptor (Zhang et al., 2006).”
• The ErbB/HER family of protein-tyrosine kinases and cancer. (2014, background): “This dimer nterface results in the burial of ≈2020 Å2 of surface area [64].”
• Overcoming EGFR T790M and C797S resistance with mutant-selective allosteric inhibitors (2016, positive): “Ligand-induced dimerization of the EGF receptor is known to induce an asymmetric interaction of the kinase domains 8 , and is an obvious potential source of two receptor populations with differential inhibitor sensitivity.”