Solution structures and biophysical analysis of full-length group A PAKs reveal they are monomeric and auto-inhibited in cis
The group A p21-activated kinases (PAKs) exist in an auto-inhibited form until activated by GTPase binding and auto-phosphorylation. In the auto-inhibited form, a regulatory domain binds to the kinase domain (KD) blocking the binding of substrates, and CDC42 or Rac binding to the regulatory domain r...
Main Authors: | Sorrell, F, Kilian, L, Elkins, J |
---|---|
Format: | Journal article |
Language: | English |
Published: |
Portland Press
2019
|
Similar Items
-
The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane
by: Zeev-Ben-Mordehai, T, et al.
Published: (2014) -
An optimized protocol for expression and purification of monomeric full-length BAX protein for functional interrogations
by: Yiyang Chen, et al.
Published: (2023-12-01) -
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs
by: Eswaran, J, et al.
Published: (2007) -
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.
by: Eswaran, J, et al.
Published: (2007) -
The structure of the full-length tetrameric PKA regulatory RIIβ complex reveals the mechanism of allosteric PKA activation.
by: Elkins, J, et al.
Published: (2012)