A comprehensive in silico exploration of the impacts of missense variants on two different conformations of human pirin protein.

ABSTRACT:

Background

Pirin, a member of the cupin superfamily, is an iron-binding non-heme protein. It acts as a coregulator of several transcription factors, especially the members of NFκB transcription factor family. Based on the redox state of its iron cofactor, it can assume two different conformations and thereby act as a redox sensor inside the nucleus. Previous studies suggested that pirin may be associated with cancer, inflammatory diseases as well as COVID-19 severities. Hence, it is important to explore the pathogenicity of its missense variants. In this study, we used a number of in silico tools to investigate the effects of missense variants of pirin on its structure, stability, metal cofactor binding affinity and interactions with partner proteins. In addition, we used protein d

SUBMITTER: Khan AS 

PROVIDER: S-EPMC9362109 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature