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New page: left|200px<br /> <applet load="2e8d" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e8d" /> '''3D Structure of amyloid protofilaments of b...
 
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[[Image:2e8d.gif|left|200px]]<br />
<applet load="2e8d" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2e8d" />
'''3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR'''<br />


==Overview==
==3D Structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR==
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.
<StructureSection load='2e8d' size='340' side='right'caption='[[2e8d]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2e8d]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8d OCA], [https://pdbe.org/2e8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8d RCSB], [https://www.ebi.ac.uk/pdbsum/2e8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8d ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>  Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
== Function ==
[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.


==Disease==
==See Also==
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
== References ==
==About this Structure==
<references/>
2E8D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E8D OCA].
__TOC__
 
</StructureSection>
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17108084 17108084]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fujiwara, T.]]
[[Category: Fujiwara T]]
[[Category: beta2-microglobulin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:46:58 2007''

Latest revision as of 06:39, 1 May 2024

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

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