From Proteopedia
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| - | [[Image:1rvs.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rvs| PDB=1rvs | SCENE= }} | | {{STRUCTURE_1rvs| PDB=1rvs | SCENE= }} |
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| - | '''STRUCTURE OF TRANSTHYRETIN IN AMYLOID FIBRILS DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR'''
| + | ===STRUCTURE OF TRANSTHYRETIN IN AMYLOID FIBRILS DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR=== |
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| - | ==Overview==
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| - | Amyloid fibrils are self-assembled filamentous structures associated with protein deposition conditions including Alzheimer's disease and the transmissible spongiform encephalopathies. Despite the immense medical importance of amyloid fibrils, no atomic-resolution structures are available for these materials, because the intact fibrils are insoluble and do not form diffraction-quality 3D crystals. Here we report the high-resolution structure of a peptide fragment of the amyloidogenic protein transthyretin, TTR(105-115), in its fibrillar form, determined by magic angle spinning NMR spectroscopy. The structure resolves not only the backbone fold but also the precise conformation of the side chains. Nearly complete (13)C and (15)N resonance assignments for TTR(105-115) formed the basis for the extraction of a set of distance and dihedral angle restraints. A total of 76 self-consistent experimental measurements, including 41 restraints on 19 backbone dihedral angles and 35 (13)C-(15)N distances between 3 and 6 A were obtained from 2D and 3D NMR spectra recorded on three fibril samples uniformly (13)C, (15)N-labeled in consecutive stretches of four amino acids and used to calculate an ensemble of peptide structures. Our results indicate that TTR(105-115) adopts an extended beta-strand conformation in the amyloid fibrils such that both the main- and side-chain torsion angles are close to their optimal values. Moreover, the structure of this peptide in the fibrillar form has a degree of long-range order that is generally associated only with crystalline materials. These findings provide an explanation of the unusual stability and characteristic properties of this form of polypeptide assembly.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14715898}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14715898 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14715898}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1RVS is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVS OCA]. | + | 1RVS is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVS OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Transthyretin]] | | [[Category: Transthyretin]] |
| | [[Category: Ttr]] | | [[Category: Ttr]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:57:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:50:02 2008'' |
Revision as of 15:50, 27 July 2008
Template:STRUCTURE 1rvs
STRUCTURE OF TRANSTHYRETIN IN AMYLOID FIBRILS DETERMINED BY SOLID-STATE MAGIC ANGLE SPINNING NMR
Template:ABSTRACT PUBMED 14715898
About this Structure
1RVS is a Single protein structure. Full experimental information is available from OCA.
Reference
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy., Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG, Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):711-6. Epub 2004 Jan 8. PMID:14715898
Page seeded by OCA on Sun Jul 27 18:50:02 2008
