KRAS Ubiquitination at Lysine 104 Retains Exchange Factor Regulation by Dynamically Modulating the Conformation of the Interface

KRAS Ubiquitination at Lysine 104 Retains Exchange Factor Regulation by Dynamically Modulating the Conformation of the Interface

Summary: RAS proteins function as highly regulated molecular switches that control cellular growth. In addition to regulatory proteins, RAS undergoes a number of posttranslational modifications (PTMs) that regulate its activity. Lysine 104, a hot spot for multiple PTMs, is a highly conserved residue...

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Bibliographic Details
Main Authors: Guowei Yin, Jerry Zhang, Vinay Nair, Vinh Truong, Angelo Chaia, Johnny Petela, Joseph Harrison, Alemayehu A. Gorfe, Sharon L. Campbell
Format: Article
Language:English
Published: Elsevier 2020-09-01
Series:iScience
Subjects:
Structural Biology
Biochemistry
Biocomputational Method
Online Access:http://www.sciencedirect.com/science/article/pii/S2589004220306404

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http://www.sciencedirect.com/science/article/pii/S2589004220306404

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