2yxf

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[[Image:2yxf.gif|left|200px]]<br /><applet load="2yxf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2yxf, resolution 1.13&Aring;" />
 
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'''The high resolution crystal structure of beta2-microglobulin under physiological conditions'''<br />
 
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==Overview==
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==The high resolution crystal structure of beta2-microglobulin under physiological conditions==
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beta(2)-Microglobulin (beta2-m), a light chain of the major, histocompatibility complex class I, forms amyloid fibrils in patients, undergoing long-term haemodialysis, causing dialysis-related amyloidosis., Based on a comparison of the X-ray structure obtained at pH 5.7 and that, of beta2-m in the histocompatibility complex, it has been proposed that, the continuous D-strand observed in the crystal structure at pH 5.7, increases the propensity of beta2-m to self-associate via edge-to-edge, interactions, thus initiating the formation of fibrils. To obtain further, insight into the mechanism by which amyloid fibrils form, we determined, the crystal structure of beta2-m at pH 7.0 at a resolution of up to 1.13, A. The crystal structure at pH 7.0 was basically the same as that at pH, 5.6, suggesting that the conversion of the beta-bulge in strand D into a, contiguous beta-strand is not unique to the crystals formed under slightly, acidic conditions. In other words, although the formation of beta2-m, fibrils was enhanced under acidic conditions, it remains unknown if it is, related to the increased propensity for the disappearance of the, beta-bulge in strand D. We consider that the enhanced fibrillation is more, directly coupled with the decreased stability leading to the increased, propensity of exposing amyloidogenic regions.
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<StructureSection load='2yxf' size='340' side='right'caption='[[2yxf]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2yxf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YXF FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.13&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxf OCA], [https://pdbe.org/2yxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yxf RCSB], [https://www.ebi.ac.uk/pdbsum/2yxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yxf ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yxf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2yxf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta(2)-Microglobulin (beta2-m), a light chain of the major histocompatibility complex class I, forms amyloid fibrils in patients undergoing long-term haemodialysis, causing dialysis-related amyloidosis. Based on a comparison of the X-ray structure obtained at pH 5.7 and that of beta2-m in the histocompatibility complex, it has been proposed that the continuous D-strand observed in the crystal structure at pH 5.7 increases the propensity of beta2-m to self-associate via edge-to-edge interactions, thus initiating the formation of fibrils. To obtain further insight into the mechanism by which amyloid fibrils form, we determined the crystal structure of beta2-m at pH 7.0 at a resolution of up to 1.13 A. The crystal structure at pH 7.0 was basically the same as that at pH 5.6, suggesting that the conversion of the beta-bulge in strand D into a contiguous beta-strand is not unique to the crystals formed under slightly acidic conditions. In other words, although the formation of beta2-m fibrils was enhanced under acidic conditions, it remains unknown if it is related to the increased propensity for the disappearance of the beta-bulge in strand D. We consider that the enhanced fibrillation is more directly coupled with the decreased stability leading to the increased propensity of exposing amyloidogenic regions.
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==About this Structure==
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High-resolution crystal structure of beta2-microglobulin formed at pH 7.0.,Iwata K, Matsuura T, Sakurai K, Nakagawa A, Goto Y J Biochem. 2007 Sep;142(3):413-9. Epub 2007 Jul 23. PMID:17646174<ref>PMID:17646174</ref>
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2YXF 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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High-resolution Crystal Structure of {beta}2-Microglobulin Formed at pH 7.0., Iwata K, Matsuura T, Sakurai K, Nakagawa A, Goto Y, J Biochem (Tokyo). 2007 Sep;142(3):413-9. Epub 2007 Jul 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17646174 17646174]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2yxf" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Goto, Y.]]
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[[Category: Iwata, K.]]
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[[Category: Matsuura, T.]]
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[[Category: Nakagawa, A.]]
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[[Category: immune system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:39:22 2008''
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==See Also==
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Goto Y]]
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[[Category: Iwata K]]
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[[Category: Matsuura T]]
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[[Category: Nakagawa A]]

Current revision

The high resolution crystal structure of beta2-microglobulin under physiological conditions

PDB ID 2yxf

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