2e8d: Difference between revisions

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[[Image:2e8d.gif|left|200px]]
{{Seed}}
[[Image:2e8d.png|left|200px]]


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{{STRUCTURE_2e8d|  PDB=2e8d  |  SCENE=  }}  
{{STRUCTURE_2e8d|  PDB=2e8d  |  SCENE=  }}  


'''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===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_17108084}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_17108084}}


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2E8D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8D OCA].  
2E8D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E8D OCA].  


==Reference==
==Reference==
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[[Category: Fujiwara, T.]]
[[Category: Fujiwara, T.]]
[[Category: Beta2-microglobulin]]
[[Category: Beta2-microglobulin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:07:44 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:34:45 2008''

Revision as of 20:34, 28 July 2008

File:2e8d.png

Template:STRUCTURE 2e8d

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

Template:ABSTRACT PUBMED 17108084

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 experimental 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 Mon Jul 28 23:34:45 2008

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