Nucleotide substrate binding characterization in human pancreatic-type ribonucleases.

ABSTRACT: Human genome contains a group of more than a dozen similar genes with diverse biological functions including antiviral, antibacterial and angiogenesis activities. The characterized gene products of this group show significant sequence similarity and a common structural fold associated with binding and cleavage of ribonucleic acid (RNA) substrates. Therefore, these proteins have been categorized as members of human pancreatic-type ribonucleases (hRNases). hRNases differ in cell/tissue localization and display distinct substrate binding preferences and a wide range of ribonucleolytic catalytic efficiencies. Limited information is available about structural and dynamical properties that influence this diversity among these homologous RNases. Here, we use computer simulations to characterize s

SUBMITTER: Bafna K 

PROVIDER: S-EPMC6687278 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature