Article
Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment.
Structure (London, England : 1993) - 7 Aug 2018
Xiong Shawn, Lorenzen Kristina, Couzens Amber L, Templeton Catherine M, Rajendran Dushyandi, Mao Daniel Y L, Juang Yu-Chi, Chiovitti David, Kurinov Igor, Guettler Sebastian, Gingras Anne-Claude, Sicheri Frank
Abstract excerpt
The human NDR family kinases control diverse aspects of cell growth, and are regulated through phosphorylation and association with scaffolds such as MOB1. Here, we report the crystal structure of the human NDR1 kinase domain in its non-phosphorylated state, revealing a fully resolved atypically long activation segment that blocks substrate binding and stabilizes a non-productive position of helix αC. Consistent...
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