Tuning Protein Autoinhibition by Domain Destabilization
Activation of many multi-domain signaling proteins requires rearrangement of autoinhibitory interdomain interactions that occlude activator binding sites. In one model for activation, the major inactive conformation exists in equilibrium with activated-like conformations that can be stabilized by li...
Main Authors: | Cho, Jae-Hyun, Muralidharan, Vasant, Vila-Perello, Miquel, Raleigh, Daniel P., Muir, Tom W., Palmer, Arthur G. |
---|---|
Format: | Online |
Language: | English |
Published: |
2011
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265570/ |
Similar Items
-
Structure of the human Parkin ligase domain in an autoinhibited state
by: Wauer, Tobias, et al.
Published: (2013) -
Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains
by: Bor, Batbileg, et al.
Published: (2012) -
Autoinhibition of the Ron receptor tyrosine kinase by the juxtamembrane domain
by: Wang, Xin, et al.
Published: (2014) -
Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins
by: David, Yael, et al.
Published: (2015) -
Streamlined Expressed
Protein Ligation Using Split
Inteins
by: Vila-Perelló, Miquel, et al.
Published: (2012)