Conserved structural topologies in RNase A-like and trypsin-like serine proteases: a sequence-based folding analysis.

ABSTRACT:

Background

Protein folding is a complex process in which amino acid sequences encode the information required for a polypeptide chain to fold into its functional three-dimensional (3D) structure. Many proteins share common substructures and recurring secondary structure elements that contribute to similar 3D folding patterns, even across different protein families. This study examines two distinct groups of proteins, the RNase A-like fold and the trypsin-like serine protease fold, classified by SCOPe. These proteins share only some substructures that contribute to their folding cores. Despite minimal sequence identity, they exhibit partial structural similarities in their 3D topologies. We used a sequence-based approach, including inter-residue average distance statistics and conta

SUBMITTER: Kabir KMA 

PROVIDER: S-EPMC12121252 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature