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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2002-12-24
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pubmed:abstractText |
We present a structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on a set of experimental constraints from solid state NMR spectroscopy. The model additionally incorporates the cross-beta structural motif established by x-ray fiber diffraction and satisfies constraints on Abeta(1-40) fibril dimensions and mass-per-length determined from electron microscopy. Approximately the first 10 residues of Abeta(1-40) are structurally disordered in the fibrils. Residues 12-24 and 30-40 adopt beta-strand conformations and form parallel beta-sheets through intermolecular hydrogen bonding. Residues 25-29 contain a bend of the peptide backbone that brings the two beta-sheets in contact through sidechain-sidechain interactions. A single cross-beta unit is then a double-layered beta-sheet structure with a hydrophobic core and one hydrophobic face. The only charged sidechains in the core are those of D23 and K28, which form salt bridges. Fibrils with minimum mass-per-length and diameter consist of two cross-beta units with their hydrophobic faces juxtaposed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12481027-10048925,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12481027-9811813
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16742-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12481027-Amino Acid Sequence,
pubmed-meshheading:12481027-Amyloid beta-Peptides,
pubmed-meshheading:12481027-Humans,
pubmed-meshheading:12481027-Models, Molecular,
pubmed-meshheading:12481027-Molecular Sequence Data,
pubmed-meshheading:12481027-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12481027-Peptide Fragments,
pubmed-meshheading:12481027-Protein Structure, Secondary
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pubmed:year |
2002
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pubmed:articleTitle |
A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.
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pubmed:affiliation |
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
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pubmed:publicationType |
Journal Article
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