Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT

Melinda M. Diver, Leanne Pedi, Akiko Koide, Shohei Koide and Stephen B. Long ()
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Melinda M. Diver: Structural Biology Program, Memorial Sloan Kettering Cancer Center
Leanne Pedi: Structural Biology Program, Memorial Sloan Kettering Cancer Center
Akiko Koide: Perlmutter Cancer Center, New York University Langone Medical Center
Shohei Koide: Perlmutter Cancer Center, New York University Langone Medical Center
Stephen B. Long: Structural Biology Program, Memorial Sloan Kettering Cancer Center

Nature, 2018, vol. 553, issue 7689, 526-529

Abstract: The X-ray structure of the integral membrane protein isoprenylcysteine carboxyl methyltransferase suggests mechanisms by which it recognizes both water-soluble and membrane-bound reactants to catalyze the methylation of RAS and other CAAX proteins at the membrane-cytosol interface.

Date: 2018
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DOI: 10.1038/nature25439

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