A Glance into MTHFR Deficiency at a Molecular Level.

ABSTRACT: MTHFR deficiency still deserves an investigation to associate the phenotype to protein structure variations. To this aim, considering the MTHFR wild type protein structure, with a catalytic and a regulatory domain and taking advantage of state-of-the-art computational tools, we explore the properties of 72 missense variations known to be disease associated. By computing the thermodynamic ΔΔG change according to a consensus method that we recently introduced, we find that 61% of the disease-related variations destabilize the protein, are present both in the catalytic and regulatory domain and correspond to known biochemical deficiencies. The propensity of solvent accessible residues to be involved in protein-protein interaction sites indicates that most of the interacting residues are locat

SUBMITTER: Savojardo C 

PROVIDER: S-EPMC8745156 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature