6c51

Cross-alpha Amyloid-like Structure alphaAmL

spinqualitylabelsall models 6c51, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6c51 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MPD, PO4 NonStd Res: ACE, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Amyloids adopt 'cross-beta' structures composed of long, twisted fibrils with beta-strands running perpendicular to the fibril axis. Recently, a toxic peptide was proposed to form amyloid-like cross-alpha structures in solution, with a planar bilayer-like assembly observed in the crystal structure. Here we crystallographically characterize designed peptides that assemble into spiraling cross-alpha amyloid-like structures, which resemble twisted beta-amyloid fibrils. The peptides form helical dimers, stabilized by packing of small and apolar residues, and the dimers further assemble into cross-alpha amyloid-like fibrils with superhelical pitches ranging from 170 A to 200 A. When a small residue that appeared critical for packing was converted to leucine, it resulted in structural rearrangement to a helical polymer. Fluorescently tagged versions of the designed peptides form puncta in mammalian cells, which recover from photobleaching with markedly different kinetics. These structural folds could be potentially useful for directing in vivo protein assemblies with predetermined spacing and stabilities. Designed peptides that assemble into cross-alpha amyloid-like structures.,Zhang SQ, Huang H, Yang J, Kratochvil HT, Lolicato M, Liu Y, Shu X, Liu L, DeGrado WF Nat Chem Biol. 2018 Jul 30. pii: 10.1038/s41589-018-0105-5. doi:, 10.1038/s41589-018-0105-5. PMID:30061717 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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