Ontology highlight
ABSTRACT:
SUBMITTER: Harrison CF
PROVIDER: S-EPMC2888434 | biostudies-literature | 2010 Jun
REPOSITORIES: biostudies-literature
Harrison Christopher F CF Lawson Victoria A VA Coleman Bradley M BM Kim Yong-Sun YS Masters Colin L CL Cappai Roberto R Barnham Kevin J KJ Hill Andrew F AF
The Journal of biological chemistry 20100331 26
Prion diseases are associated with the misfolding of the endogenously expressed prion protein (designated PrP(C)) into an abnormal isoform (PrP(Sc)) that has infectious properties. The hydrophobic domain of PrP(C) is highly conserved and contains a series of glycine residues that show perfect conservation among all species, strongly suggesting it has functional and evolutionary significance. These glycine residues appear to form repeats of the GXXXG protein-protein interaction motif (two glycine ...[more]