PDBsum entry 4tut

Membrane protein, de novo protein

PDB id: 4tut

Contents

Ligands

GLY-GLY-TYR-MET-LEU-GLY

Waters ×5

PDB id:

4tut

Name:

Membrane protein, de novo protein

Title:

Structure of a prion peptide

Structure:

Prion peptide: gly-gly-tyr-met-leu-gly. Chain: a. Engineered: yes

Source:

Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

0.90Å R-factor: 0.071 R-free: 0.098

Authors:

L.Yu,S.-J.Lee,V.Yee

Key ref:

L.Yu et al. (2015). Crystal Structures of Polymorphic Prion Protein β1 Peptides Reveal Variable Steric Zipper Conformations. Biochemistry, 54, 3640-3648. PubMed id: 25978088 DOI: 10.1021/acs.biochem.5b00425

Date:

24-Jun-14 Release date: 27-May-15

DOI no: 10.1021/acs.biochem.5b00425

Biochemistry 54:3640-3648 (2015)

PubMed id: 25978088

Crystal Structures of Polymorphic Prion Protein β1 Peptides Reveal Variable Steric Zipper Conformations.

L.Yu, S.J.Lee, V.C.Yee.

ABSTRACT

The pathogenesis of prion diseases is associated with the conformational conversion of normal, predominantly α-helical prion protein (PrP(C)) into a pathogenic form that is enriched with β-sheets (PrP(Sc)). Several PrP(C) crystal structures have revealed β1-mediated intermolecular sheets, suggesting that the β1 strand may contribute to a possible initiation site for β-sheet-mediated PrP(Sc) propagation. This β1 strand contains the polymorphic residue 129 that influences disease susceptibility and phenotype. To investigate the effect of the residue 129 polymorphism on the conformation of amyloid-like continuous β-sheets formed by β1, crystal structures of β1 peptides containing each of the polymorphic residues were determined. To probe the conformational influence of the peptide construct design, four different lengths of β1 peptides were studied. From the 12 peptides studied, 11 yielded crystal structures ranging in resolution from 0.9 to 1.4 Å. This ensemble of β1 crystal structures reveals conformational differences that are influenced by both the nature of the polymorphic residue and the extent of the peptide construct, indicating that comprehensive studies in which peptide constructs vary are a more rigorous approach to surveying conformational possibilities.