2e8d

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[[Image:2e8d.gif|left|200px]]
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{{Structure
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|GENE= B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8d OCA], [http://www.ebi.ac.uk/pdbsum/2e8d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e8d RCSB]</span>
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'''3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR'''
'''3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fujiwara, T.]]
[[Category: Fujiwara, T.]]
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[[Category: beta2-microglobulin]]
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[[Category: Beta2-microglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:07:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:15 2008''
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Revision as of 23:07, 3 May 2008

Template:STRUCTURE 2e8d

3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR


Contents

Overview

Understanding the structure and formation of amyloid fibrils, the filamentous aggregates of proteins and peptides, is crucial in preventing diseases caused by their deposition and, moreover, for obtaining further insight into the mechanism of protein folding and misfolding. We have combined solid-state NMR, x-ray fiber diffraction, and atomic force microscopy to reveal the 3D structure of amyloid protofilament-like fibrils formed by a 22-residue K3 peptide (Ser(20)-Lys(41)) of beta(2)-microglobulin, a protein responsible for dialysis-related amyloidosis. Although a uniformly (13)C,(15)N-labeled sample was used for the NMR measurements, we could obtain the 3D structure of the fibrils on the basis of a large number of structural constraints. The conformation of K3 fibrils was found to be a beta-strand-loop-beta-strand with each K3 molecule stacked in a parallel and staggered manner. It is suggested that the fibrillar conformation is stabilized by intermolecular interactions, rather than by intramolecular hydrophobic packing as seen in globular proteins. Together with thermodynamic studies of the full-length protein, formation of the fibrils is likely to require side chains on the intermolecular surface to pack tightly against those of adjacent monomers. By revealing the structure of beta(2)-microglobulin protofilament-like fibrils, this work represents technical progress in analyzing amyloid fibrils in general through solid-state NMR.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

2E8D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR., Iwata K, Fujiwara T, Matsuki Y, Akutsu H, Takahashi S, Naiki H, Goto Y, Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18119-24. Epub 2006 Nov 15. PMID:17108084 Page seeded by OCA on Sun May 4 02:07:44 2008

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