Related ArticlesSolid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Nat Struct Mol Biol. 2016 Mar 28;
Authors: Tuttle MD, Comellas G, Nieuwkoop AJ, Covell DJ, Berthold DA, Kloepper KD, Courtney JM, Kim JK, Barclay AM, Kendall A, Wan W, Stubbs G, Schwieters CD, Lee VM, George JM, Rienstra CM
Abstract
Misfolded ?-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of Parkinson's disease (PD). We present a high-resolution structure of an ?-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction. Over 200 unique long-range distance restraints define a consensus structure with common amyloid features including parallel, in-register ?-sheets and hydrophobic-core residues, and with substantial complexity arising from diverse structural features including an intermolecular salt bridge, a glutamine ladder, close backbone interactions involving small residues, and several steric zippers stabilizing a new orthogonal Greek-key topology. These characteristics contribute to the robust propagation of this fibril form, as supported by the structural similarity of early-onset-PD mutants. The structure provides a framework for understanding the interactions of ?-synuclein with other proteins and small molecules, to aid in PD diagnosis and treatment.
PMID: 27018801 [PubMed - as supplied by publisher]
[NMR paper] Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
J Am Chem Soc. 2014 Nov 10;
Authors: Lamley JM, Iuga D, Oster C, Sass HJ, Rogowski M, Oss A, Past J, Reinhold A, Grzesiek S, Samoson A, Lewandowski JR
Abstract
NMR is a prime technique for characterizing atomic resolution structures and dynamics of biomolecular complexes but, for such systems, faces challenges of sensitivity and spectral resolution. We...
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11-11-2014 11:57 AM
[NMR paper] Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
Related Articles Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
J Mol Biol. 2014 Feb 12;
Authors: Sinnige T, Weingarth M, Renault M, Baker L, Tommassen J, Baldus M
Abstract
The outer membrane protein BamA is the key player in ?-barrel assembly in Gram-negative bacteria. Despite the availability of high-resolution crystal structures, the dynamic behavior of the transmembrane domain and...
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02-19-2014 12:07 AM
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane helix and an adjacent amphipathic helix, the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using two-dimensional (2D) magic-angle-spinning solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
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[NMR paper] Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Protein Sci. 2013 Sep 10;
Authors: Liao SY, Fritzsching KJ, Hong M
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus...
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09-12-2013 11:02 PM
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane (TM) helix and an adjacent amphipathic helix (AH), the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using 2D magic-angle-spinning (MAS) solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
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09-10-2013 08:44 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Biomol NMR Assign. 2013 Aug 14;
Authors: Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH
Abstract
Sup35p is a yeast prion and is responsible for the trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated...
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08-15-2013 07:45 PM
[NMR paper] Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Related Articles Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
FEBS J. 2013 Apr 20;
Authors: Renault M, García J, Cordeiro TN, Baldus M, Pons M
Abstract
Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes...
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04-23-2013 08:37 PM
[NMR paper] Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscop
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
Related Articles Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
J Biomed Sci. 2005;12(3):451-6
Authors: Briese L, Preusser A, Willbold D
The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. To address the question whether Nef binding to Lck SH3 involves...
Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Linear Mode
