ArticleBiochemistry2010
High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Isoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR.Journal of the American Chemical Society · 2025Article
- Amyloid fibril formation kinetics of low-pH denatured bovine PI3K-SH3 monitored by three different NMR techniques.Frontiers in molecular biosciences · 2023Article
- Extensively sparseJournal of biomolecular NMR · 2021Article
- Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy.Nature communications · 2019Article
- Aggregation and Fibril Structure of AβBiochemistry · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Journal of the American Chemical Society · 2016Article
- Dynamic nuclear polarization of nucleic acid with endogenously bound manganese.Journal of biomolecular NMR · 2015Article
- High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Journal of the American Chemical Society · 2015Article
- Physical and structural basis for polymorphism in amyloid fibrils.Protein science : a publication of the Protein Society · 2014Review
- Solid-state NMR studies of metal-free SOD1 fibrillar structures.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- Topical Developments in High-Field Dynamic Nuclear Polarization.Israel journal of chemistry · 2014Article
- Article
- Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Journal of the American Chemical Society · 2013Article
- Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR.Journal of biomolecular NMR · 2013Article
- High frequency dynamic nuclear polarization.Accounts of chemical research · 2013Article
- Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Journal of biomolecular NMR · 2013Article
- Continuously Tunable 250 GHz Gyrotron with a Double Disk Window for DNP-NMR Spectroscopy.Journal of infrared, millimeter and terahertz waves · 2013Article
- Dynamic nuclear polarization at 700 MHz/460 GHz.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
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6 authors.
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Abstract
The SH3 domain of the PI3 kinase (PI3-SH3 or PI3K-SH3) readily aggregates into fibrils in vitro and has served as an important model system in the investigation of the molecular properties and mechanism of formation of amyloid fibrils. We describe the molecular conformation of PI3-SH3 in amyloid fibril form as revealed by magic-angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) spectroscopy. The MAS NMR spectra of these fibrils display excellent resolution, with narrow (13)C and (15)N line widths, representing a high degree of structural order and the absence of extensive molecular motion for the majority of the polypeptide chain. We have identified the spin systems of 82 of the 86 residues in the protein and obtained sequential resonance assignments for 75 of them. Chemical shift analysis indicates that the protein subunits making up the fibril adopt a compact conformation consisting of four well-defined beta-sheet regions and four random-coil elements with varying degrees of local dynamics or disorder. The backbone conformation of PI3-SH3 in fibril form differs significantly from that of the native state of the protein, both in secondary structure and in the location of dynamic or disordered segments. The site-specific MAS NMR analysis of PI3-SH3 fibrils we report here is compared with previously published mechanistic and structural data, resulting in a detailed interpretation of the factors that mediate fibril formation by PI3-SH3 and allowing us to propose a possible model of the core structure of the fibrils. Our results confirm the structural similarities between PI3-SH3 fibrils and amyloid assemblies directly related to degenerative and infectious diseases.
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