Cooperative dynamics across distinct structural elements regulate PTP1B activity.

ABSTRACT: Protein-tyrosine phosphatase 1B (PTP1B) is the canonical enzyme for investigating how distinct structural elements influence enzyme catalytic activity. Although it is recognized that dynamics are essential for PTP1B function, the data collected thus far have not resolved whether distinct elements are dynamically coordinated or, alternatively, whether they fulfill their respective functions independently. To answer this question, we performed a comprehensive ¹³C-methyl relaxation study of Ile, Leu, and Val (ILV) residues of PTP1B, which, because of its substantially increased sensitivity, provides a comprehensive understanding of the influence of protein motions on different time scales for enzyme function. We discovered that PTP1B exhibits dynamics at three distinct time scales.

SUBMITTER: Torgeson KR 

PROVIDER: S-EPMC7535920 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature