5hpp | pdb_00005hpp

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

spinqualitylabelsall models 5hpp, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hpp is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL NonStd Res: MAA, ORN, PHI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-sheet peptide derived from transthyretin (TTR). The peptide mimics the beta-hairpin formed by the beta-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 beta-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 beta-sheets. Square channels formed by a peptide derived from transthyretin.,Yoo S, Kreutzer AG, Truex NL, Nowick JS Chem Sci. 2016 Dec 1;7(12):6946-6951. doi: 10.1039/c6sc01927g. Epub 2016 Aug 1. PMID:28451128 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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