Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood.

In primary biliary cholangitis, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed.

The composition of E2.E3BP was thought to be 60 E2 plus approximately 12 E3BP, however, equilibrium sedimentation and small angle x-ray scattering studies showed that the E3BP/E2 binding complex has a lower mass than the E2 subunit alone.

[12] This has also shown that E3BP has residues that come into contact with the E3 component across its two-fold axis; this means that there is one binding site for this reaction on the E3 homodimer.

This specificity is most likely due to the lack of conformational flexibility of the binding fragment of E3BP and the complementary amino acid match with the E3 interface.

Pyruvate dehydrogenase deficiency is characterized by the buildup of a chemical called lactic acid in the body and a variety of neurological problems.

Other neurological problems can include intellectual disability, seizures, weak muscle tone (hypotonia), poor coordination, and difficulty walking.

Because of the severe health effects, many individuals with pyruvate dehydrogenase deficiency do not survive past childhood, although some may live into adolescence or adulthood.

[§ 1] This article incorporates text from the United States National Library of Medicine, which is in the public domain.