Pepsin-like aspartic proteases (PAPs) as model systems for combining biomolecular simulation with biophysical experiments.

ABSTRACT: Pepsin-like aspartic proteases (PAPs) are a class of aspartic proteases which shares tremendous structural similarity with human pepsin. One of the key structural features of PAPs is the presence of a β-hairpin motif otherwise known as flap. The biological function of the PAPs is highly dependent on the conformational dynamics of the flap region. In apo PAPs, the conformational dynamics of the flap is dominated by the rotational degrees of freedom associated with χ1 and χ2 angles of conserved Tyr (or Phe in some cases). However it is plausible that dihedral order parameters associated with several other residues might play crucial roles in the conformational dynamics of apo PAPs. Due to their size, complexities associated with conformational dynamics and clinical significance

SUBMITTER: Bhakat S 

PROVIDER: S-EPMC8695779 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature