2021
DOI: 10.1080/21541248.2021.1979360
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KRAS G12C fragment screening renders new binding pockets

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Cited by 15 publications
(8 citation statements)
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“…Attempts to target mutant KRAS and its downstream mediators in cancer therapy remain largely unsuccessful [4,22]. However, two inhibitors efficiently targeting mutant KRAS-G12C have been developed but the clinical efficacy is yet to be determined in ongoing trials [23][24][25][26][27]. Concurrently, it has been suggested that NSCLC harboring KRAS mutations might benefit from ICB therapy compared to KRAS wild type tumors [28].…”
mentioning
confidence: 99%
“…Attempts to target mutant KRAS and its downstream mediators in cancer therapy remain largely unsuccessful [4,22]. However, two inhibitors efficiently targeting mutant KRAS-G12C have been developed but the clinical efficacy is yet to be determined in ongoing trials [23][24][25][26][27]. Concurrently, it has been suggested that NSCLC harboring KRAS mutations might benefit from ICB therapy compared to KRAS wild type tumors [28].…”
mentioning
confidence: 99%
“…Clustering of the ligands reveals three clusters (A, B, and C), representing three different binding modes, including the substantial allosteric effect of this binding site (Figure b). In Cluster-A, the ligand QY5 binds into one end of the Class-III binding site between the P-loop, Switch-I, and Switch-II and has no interactions with helix α3 (Figure c) . Indeed, Switch-I deviates away from helix α3 (Figure c).…”
Section: Resultsmentioning
confidence: 99%
“…Clustering of the ligands reveals three clusters (A, B, and C), representing three different binding modes, including the substantial allosteric effect of this binding site (Figure 5b). In Cluster-A, the ligand QY5 binds into one end of the Class-III binding site between the P-loop, Switch-I, and Switch-II, and has no interactions with helix α3 (Figure 5c) 32 . Indeed, Switch-I deviates away from helix α3 (Figure 3c).…”
Section: Resultsmentioning
confidence: 99%