A method to trap transient and weak interacting protein complexes for structural studies.

ABSTRACT: Several key biological events adopt a "hit-and-run" strategy in their transient interactions between binding partners. In some instances, the disordered nature of one of the binding partners severely hampers the success of co-crystallization, often leading to the crystallization of just one of the partners. Here, we discuss a method to trap weak and transient protein interactions for crystallization. This approach requires the structural details of at least one of the interacting partners and binding knowledge to dock the known minimum binding region (peptide) of the protein onto the other using an optimal-sized linker. Prior to crystallization, the purified linked construct should be verified for its intact folding and stability. Following structure determination, structure-guided functio

SUBMITTER: Chichili VPR 

PROVIDER: S-EPMC5424782 | biostudies-literature | 2013 Jan-Dec

REPOSITORIES: biostudies-literature