Cited by 163Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

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The reactivity-driven biochemical mechanism of covalent KRASG12C inhibitors

Hansen, Rasmus, Peters, Ulf, Babbar, Anjali, Chen, Yuching, Feng, Jun, Janes, Matthew R., Li, Lian-Sheng, Ren, Pingda, Liu, Yi, Zarrinkar, Patrick P.·2018·Nature Structural & Molecular Biology

DOI 10.1038/s41594-018-0061-5

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Abstract

Activating mutations in KRAS are among the most common tumor driver mutations. Until recently, KRAS had been considered undruggable with small molecules; the discovery of the covalent KRAS G12C inhibitors ARS-853 and ARS-1620 has demonstrated that it is feasible to inhibit KRAS with high potency in cells and animals. Although the biological activity of these inhibitors has been described, the biochemical mechanism of how the compounds achieve potent inhibition remained incompletely understood. We now show that the activity of ARS-853 and ARS-1620 is primarily driven by KRAS-mediated catalysis of the chemical reaction with Cys12 in human KRAS G12C, while the reversible binding affinity is weak, in the hundreds of micromolar or higher range. The mechanism resolves how an induced, shallow and dynamic pocket not expected to support high-affinity binding of small molecules can nevertheless be targeted with potent inhibitors and may be applicable to other targets conventionally considered undruggable.

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BindingDB Entry 50015318: Identification of MRTX1133, a Noncovalent, Potent, and Selective KRAS
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BindingDB Entry 50009311: Structure-Based Design and Pharmacokinetic Optimization of Covalent Allosteric Inhibitors of the Mutant GTPase KRAS
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BindingDB Entry 50017120: Drugging the Next Undruggable KRAS Allele-Gly12Asp.
BindingDB (2023) · UC San Diego · doi:10.7270/q25b06j8
BindingDB Entry 50011605: Small-Molecule Inhibitors Directly Targeting KRAS as Anticancer Therapeutics.
BindingDB (2022) · UC San Diego · doi:10.7270/q2t1578s

Authors: Hansen, R., Peters, U., Babbar, A., Chen, Y., Feng, J., Janes, M. R., Li, L.-S., Ren, P., Liu, Y., & Zarrinkar, P. P.
Affiliations: Wellspring Biosciences (United States) (US)
Kura Oncology (United States) (US)
Corresponding author: Zarrinkar, Patrick P.
ORCID: Peters, Ulf
Janes, Matthew R.
Li, Lian-Sheng
Ren, Pingda
Liu, Yi
Zarrinkar, Patrick P.
Venue: Nature Structural & Molecular Biology
Publisher: Springer Science and Business Media LLC
Published: 2018-05-14
Volume: 25
Issue: 6
Pages: 454-462
ISSN: 1545-9985 (ISSN-L)
1545-9993
DOI: 10.1038/s41594-018-0061-5
OpenAlex: W2800484366
Cited by: 153
References: 39
Citations by year: 2026: 14 · 2025: 18 · 2024: 20 · 2023: 16 · 2022: 20 · 2021: 15 · 2020: 25 · 2019: 19 · 2018: 5
FWCI: 6.22
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Structural & Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords: KRAS G12C, covalent inhibitors, undruggable targets, enzyme kinetics, small molecule inhibitors
MeSH terms: Animals, Catalysis, Cysteine, Humans, Kinetics, Mutation, Neoplasms, Protein Binding, Genes, ras, ras Proteins

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The reactivity-driven biochemical mechanism of covalent KRASG12C inhibitors

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