5HPP

Crystal structure of a macrocyclic beta-sheet peptide derived from transthyretin (106-121) - (ORN)TIA(MAA)LLS(ORN)S(PHI)STTAV

Summary for 5HPP

• Entry DOI: 10.2210/pdb5hpp/pdb
• Descriptor: ORN-THR-ILE-ALA-MAA-LEU-LEU-SER-ORN-SER-PHI-SER-THR-THR-ALA-VAL, CHLORIDE ION (3 entities in total)
• Functional Keywords: beta-hairpin, nanotube assembly, de novo protein
• Biological source: Homo sapiens
• Total number of polymer chains: 1
• Total formula weight: 1785.24

Authors

Yoo, S.,Kreutzer, A.G.,Nowick, J.S. (deposition date: 2016-01-20, release date: 2016-08-10, Last modification date: 2025-04-02)

Primary citation

Yoo, S.,Kreutzer, A.G.,Truex, N.L.,Nowick, J.S.
Square channels formed by a peptide derived from transthyretin.
Chem Sci, 7:6946-6951, 2016

PubMed 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.

PubMed: 28451128
DOI: 10.1039/c6sc01927g

Experimental method

X-RAY DIFFRACTION (2.082 Å)