Molecular properties of wild-type and mutant betaIG-H3 proteins.

Abstract

BetaIG-H3 polymerizes to form a fibrillar structure and strongly interacts with type I collagen, laminin, and fibronectin. Mutations found in the 5q31-linked corneal dystrophies do not significantly affect these properties. The results suggest that mutant forms of betaIG-H3 may require other cornea-specific factors, to form the abnormal accumulations in 5q31-linked corneal dystrophies.