Direct visualization reveals dynamics of a transient intermediate during protein assembly.

ABSTRACT: Interactions between proteins underlie numerous biological functions. Theoretical work suggests that protein interactions initiate with formation of transient intermediates that subsequently relax to specific, stable complexes. However, the nature and roles of these transient intermediates have remained elusive. Here, we characterized the global structure, dynamics, and stability of a transient, on-pathway intermediate during complex assembly between the Signal Recognition Particle (SRP) and its receptor. We show that this intermediate has overlapping but distinct interaction interfaces from that of the final complex, and it is stabilized by long-range electrostatic interactions. A wide distribution of conformations is explored by the intermediate; this distribution becomes more restricted

SUBMITTER: Zhang X 

PROVIDER: S-EPMC3081034 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature