Molecular Dynamics Studies of Dog Prion Protein Wild-type and Its D159N Mutant

Abstract

Prion diseases (e.g. "mad cow" disease in cattle, chronic wasting disease in deer and elk, CJD in humans) have been a major public health concern affecting humans and almost all animals. However, dogs are strongly resistant to prion diseases. Recently, it was reported that the single (surface) residue D159 is sufficient to confer protection against protein conformational change and pathogenesis, providing conformational stability for dog prion protein (Neurobiology of Disease Volume 95 (November 2016) pages 204-209). This paper studies dog prion protein wild-type and D159N mutant through molecular dynamics techniques. Molecular dynamics results reveal sufficient structural informatics on the residue at position 159 to understand the mechanism underlying the resistance to prion diseases of dogs.