Conserved patterns and interactions in the unfolding transition state across SH3 domain structural homologues.

ABSTRACT: Proteins with similar structures are generally assumed to arise from similar sequences. However, there are more cases than not where this is not true. The dogma is that sequence determines structure; how, then, can very different sequences fold to the same structure? Here, we employ high temperature unfolding simulations to probe the pathways and specific interactions that direct the folding and unfolding of the SH3 domain. The SH3 metafold in the Dynameomics Database consists of 753 proteins with the same structure, but varied sequences and functions. To investigate the relationship between sequence and structure, we selected 17 targets from the SH3 metafold with high sequence variability. Six unfolding simulations were performed for each target, transition states were identified, reveali

SUBMITTER: Demakis C 

PROVIDER: S-EPMC7784764 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature