High-throughput structure determination of an intrinsically disordered protein using cell-free protein crystallization.

ABSTRACT: Intrinsically disordered proteins (IDPs) play a crucial role in various biological phenomena, dynamically changing their conformations in response to external environmental cues. To gain a deeper understanding of these proteins, it is essential to identify the determinants that fix their structures at the atomic level. Here, we developed a pipeline for rapid crystal structure analysis of IDP using a cell-free protein crystallization (CFPC) method. Through this approach, we successfully demonstrated the determination of the structure of an IDP to uncover the key determinants that stabilize its conformation. Specifically, we focused on the 11-residue fragment of c-Myc, which forms an α-helix through dimerization with a binding partner protein. This fragment was strategically recombined with

SUBMITTER: Kojima M 

PROVIDER: S-EPMC11194560 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature