Structural basis of substrate specificity in human cytidine deaminase family APOBEC3s.

ABSTRACT: The human cytidine deaminase family of APOBEC3s (A3s) plays critical roles in both innate immunity and the development of cancers. A3s comprise seven functionally overlapping but distinct members that can be exploited as nucleotide base editors for treating genetic diseases. Although overall structurally similar, A3s have vastly varying deamination activity and substrate preferences. Recent crystal structures of ssDNA-bound A3s together with experimental studies have provided some insights into distinct substrate specificities among the family members. However, the molecular interactions responsible for their distinct biological functions and how structure regulates substrate specificity are not clear. In this study, we identified the structural basis of substrate specificities in three ca

SUBMITTER: Hou S 

PROVIDER: S-EPMC8313598 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature