In silico predicted structural and functional insights of all missense mutations on 2B domain of K1/K10 causing genodermatoses.

ABSTRACT: The K1 and K10 associated genodermatoses are characterized by clinical symptoms of mild to severe redness, blistering and hypertrophy of the skin. In this paper, we set out to computationally investigate the structural and functional effects of missense mutations on the 2B domain of K1/K10 heterodimer and its consequences in disease phenotype. We modeled the structure of the K1/K10 heterodimer based on crystal structures for the human homolog K5/K14 heterodimer, and identified that the missense mutations exert their effects on stability and assembly competence of the heterodimer by altering physico-chemical properties, interatomic interactions, and inter-residue atomic contacts. Comparative structural analysis between all the missense mutations and SNPs showed that the location and physico

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC5288147 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature