Evolution shapes interaction patterns for epistasis and specific protein binding in a two-component signaling system.

ABSTRACT: The elegant design of protein sequence/structure/function relationships arises from the interaction patterns between amino acid positions. A central question is how evolutionary forces shape the interaction patterns that encode long-range epistasis and binding specificity. Here, we combined family-wide evolutionary analysis of natural homologous sequences and structure-oriented evolution simulation for two-component signaling (TCS) system. The magnitude-frequency relationship of coupling conservation between positions manifests a power-law-like distribution and the positions with highly coupling conservation are sparse but distributed intensely on the binding surfaces and hydrophobic core. The structure-specific interaction pattern involves further optimization of local frustrations at or

SUBMITTER: Yan Z 

PROVIDER: S-EPMC10794238 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature