What the protein data bank tells us about the evolutionary conservation of protein conformational diversity.

ABSTRACT: Proteins sample a multitude of different conformations by undergoing small- and large-scale conformational changes that are often intrinsic to their functions. Information about these changes is often captured in the Protein Data Bank by the apparently redundant deposition of independent structural solutions of identical proteins. Here, we mine these data to examine the conservation of large-scale conformational changes between homologous proteins. This is important for both practical reasons, such as predicting alternative conformations of a protein by comparative modeling, and conceptual reasons, such as understanding the extent of conservation of different features in evolution. To study this question, we introduce a novel approach to compare conformational changes between proteins by t

SUBMITTER: Iyer M 

PROVIDER: S-EPMC9207624 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature