Atypical structural tendencies among low-complexity domains in the Protein Data Bank proteome.

ABSTRACT: A variety of studies have suggested that low-complexity domains (LCDs) tend to be intrinsically disordered and are relatively rare within structured proteins in the Protein Data Bank (PDB). Although LCDs are often treated as a single class, we previously found that LCDs enriched in different amino acids can exhibit substantial differences in protein metabolism and function. Therefore, we wondered whether the structural conformations of LCDs are likewise dependent on which specific amino acids are enriched within each LCD. Here, we directly examined relationships between enrichment of individual amino acids and secondary structure tendencies across the entire PDB proteome. Secondary structure tendencies varied as a function of the identity of the amino acid enriched and its degree of enrich

SUBMITTER: Cascarina SM 

PROVIDER: S-EPMC7004392 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature