A novel strategy for molecular interfaces optimization: The case of Ferritin-Transferrin receptor interaction.

ABSTRACT: Protein-protein interactions regulate almost all cellular functions and rely on a fine tune of surface amino acids properties involved on both molecular partners. The disruption of a molecular association can be caused even by a single residue mutation, often leading to a pathological modification of a biochemical pathway. Therefore the evaluation of the effects of amino acid substitutions on binding, and the ad hoc design of protein-protein interfaces, is one of the biggest challenges in computational biology. Here, we present a novel strategy for computational mutation and optimization of protein-protein interfaces. Modeling the interaction surface properties using the Zernike polynomials, we describe the shape and electrostatics of binding sites with an ordered set of descriptors

SUBMITTER: Di Rienzo L 

PROVIDER: S-EPMC7548301 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature