The The non-synonymous polymorphism Glu320Pro affects the functional stability and secondary structural conformation of the goat mature GDF9 protein

Abstract

The purpose of this study was to comparatively assess the effects of the polymorphism Glu320Pro on structural and functional stabilities, and secondary structural conformation in the goat mature GDF9 protein by in silico comparative protein prediction analyses. A wild sequence of amino acid residues of the goat GDF9 protein (Capra hircus, Q66NC0) searched from biological database and a mutant sequence harboring the substitution of the glutamine to proline residues at position 320 (polymorphic Glu320Pro) were selected. The polymorphism Glu320Pro resulted in damages in the functional and structural stabilities of the goat GDF9. Variations in the secondary structure demonstrated the presence of an alpha helix motif (H) and a coiled coil domain (C) in target position of wild and mutant GDF9, respectively. These findings suggest that the differentiated conformational pattern of the mutant GDF9 protein may exert influences on its biological action during folliculogenesis in goats.