Molecular Features of the Zn²⁺ Binding Site in the Prion Protein Probed by ¹¹³Cd NMR.

ABSTRACT: The cellular prion protein (PrP^C) is a zinc-binding protein that contributes to the regulation of Zn²⁺ and other divalent species of the central nervous system. Zn²⁺ coordinates to the flexible, N-terminal repeat region of PrP^C and drives a tertiary contact between this repeat region and a well-defined cleft of the C-terminal domain. The tertiary structure promoted by Zn²⁺ is thought to regulate inherent PrP^C toxicity. Despite the emerging consensus regarding the interaction between Zn²⁺ and PrP^C, there is little direct spectroscopic confirmation of the metal ion's coordination details. Here, we address this conceptual gap by using Cd²⁺ as a surrogate for Zn²⁺. NMR finds that Cd

SUBMITTER: Markham KA 

PROVIDER: S-EPMC6382851 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature