Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins.

ABSTRACT: The α/β-hydrolase fold superfamily of proteins is composed of structurally related members that, despite great diversity in their catalytic, recognition, adhesion and chaperone functions, share a common fold governed by homologous residues and conserved disulfide bridges. Non-synonymous single nucleotide polymorphisms within the α/β-hydrolase fold domain in various family members have been found for congenital endocrine, metabolic and nervous system disorders. By examining the amino acid sequence from the various proteins, mutations were found to be prevalent in conserved residues within the α/β-hydrolase fold of the homologous proteins. This is the case for the thyroglobulin mutations linked to congenital hypothyroidism. To address whether correct folding of the common domain is required

SUBMITTER: De Jaco A 

PROVIDER: S-EPMC5582341 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature