PDBsum entry 5hpp

De novo protein

PDB id: 5hpp

Contents

Protein chain

16 a.a.

Metals

_CL

Waters ×14

PDB id:

5hpp

Name:

De novo protein

Title:

Crystal structure of a macrocyclic beta-sheet peptide derived from transthyretin (106-121) - (orn)tia(maa)lls(orn)s(phi)sttav

Structure:

Orn-thr-ile-ala-maa-leu-leu-ser-orn-ser-phi-ser-thr-thr- ala-val. Chain: a. Engineered: yes

Source:

Synthetic: yes. Homo sapiens. Organism_taxid: 9606

Resolution:

2.08Å R-factor: 0.162 R-free: 0.184

Authors:

S.Yoo,A.G.Kreutzer,J.S.Nowick

Key ref:

S.Yoo et al. (2016). Square channels formed by a peptide derived from transthyretin. Chem Sci, 7, 6946-6951. PubMed id: 28451128

Date:

20-Jan-16 Release date: 10-Aug-16

Protein chain

No UniProt id for this chain

Struc: 16 a.a.

Chem Sci 7:6946-6951 (2016)

PubMed id: 28451128

Square channels formed by a peptide derived from transthyretin.

S.Yoo, A.G.Kreutzer, N.L.Truex, J.S.Nowick.

ABSTRACT

High-resolution structures of peptide supramolecular assemblies are key to understanding amyloid diseases and designing peptide-based materials. This paper explores the supramolecular assembly of a macrocyclic β-sheet peptide derived from transthyretin (TTR). The peptide mimics the β-hairpin formed by the β-strands G and H of TTR, which form the interface of the TTR tetramer. X-ray crystallography reveals that the peptide does not form a tetramer, but rather assembles to form square channels. The square channels are formed by extended networks of β-sheets and pack in a "tilted windows" pattern. This unexpected structure represents an emergent property of the peptide and broadens the scope of known supramolecular assemblies of β-sheets.