2xks: Difference between revisions

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-[[Image:2xks.jpg|left|200px]]
-<!--
+==Prion-like conversion during amyloid formation at atomic resolution==
-The line below this paragraph, containing "STRUCTURE_2xks", creates the "Structure Box" on the page.
+<StructureSection load='2xks' size='340' side='right'caption='[[2xks]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2xks]] is a 1 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=2XKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XKS FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</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=2xks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xks OCA], [https://pdbe.org/2xks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xks RCSB], [https://www.ebi.ac.uk/pdbsum/2xks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xks ProSAT]</span></td></tr>
-{{STRUCTURE_2xks|  PDB=2xks  |  SCENE=  }}
+</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.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Numerous studies of amyloid assembly have indicated that partially folded protein species are responsible for initiating aggregation. Despite their importance, the structural and dynamic features of amyloidogenic intermediates and the molecular details of how they cause aggregation remain elusive. Here, we use DeltaN6, a truncation variant of the naturally amyloidogenic protein beta(2)-microglobulin (beta(2)m), to determine the solution structure of a nonnative amyloidogenic intermediate at high resolution. The structure of DeltaN6 reveals a major repacking of the hydrophobic core to accommodate the nonnative peptidyl-prolyl trans-isomer at Pro32. These structural changes, together with a concomitant pH-dependent enhancement in backbone dynamics on a microsecond-millisecond timescale, give rise to a rare conformer with increased amyloidogenic potential. We further reveal that catalytic amounts of DeltaN6 are competent to convert nonamyloidogenic human wild-type beta(2)m (Hbeta(2)m) into a rare amyloidogenic conformation and provide structural evidence for the mechanism by which this conformational conversion occurs.
-===PRION-LIKE CONVERSION DURING AMYLOID FORMATION AT ATOMIC RESOLUTION===
+Conformational Conversion during Amyloid Formation at Atomic Resolution.,Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE Mol Cell. 2011 Jan 21;41(2):161-72. PMID:21255727<ref>PMID:21255727</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2xks" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21255727}}, adds the Publication Abstract to the page
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21255727 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21255727}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[2xks]] is a 1 chain structure with 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=2XKS OCA].
-==Reference==
-<ref group="xtra">PMID:21255727</ref><ref group="xtra">PMID:19452600</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Eichner, T.]]
+[[Category: Large Structures]]
-[[Category: Homans, S W.]]
+[[Category: Eichner T]]
-[[Category: Kalverda, A P.]]
+[[Category: Homans SW]]
-[[Category: Radford, S E.]]
+[[Category: Kalverda AP]]
-[[Category: Thompson, G S.]]
+[[Category: Radford SE]]
+[[Category: Thompson GS]]