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3ciq
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ciq.png|left|200px]] | ||
| - | + | ==A regulatable switch mediates self-association in an immunoglobulin fold== | |
| - | + | <StructureSection load='3ciq' size='340' side='right'caption='[[3ciq]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ciq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CIQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | |
| - | - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f8o|2f8o]]</div></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B2M ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ciq OCA], [https://pdbe.org/3ciq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ciq RCSB], [https://www.ebi.ac.uk/pdbsum/3ciq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ciq 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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/3ciq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3ciq ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Beta-2 microglobulin (beta2m) is a globular protein that self-associates into fibrillar amyloid deposits in patients undergoing hemodialysis therapy. Formation of these beta-sheet-rich assemblies is a fundamental property of polypeptides that can be triggered by diverse conditions. For beta2m, oligomerization into pre-amyloidogenic states occurs in specific response to coordination by Cu2+. Here we report the basis for this self-association at atomic resolution. Metal is not a direct participant in the molecular interface. Rather, binding results in distal alterations enabling the formation of two new surfaces. These interact to form a closed hexameric species. The origins of this include isomerization of a buried and conserved cis-proline previously implicated in the beta2m aggregation pathway. The consequences of this isomerization are evident and reveal a molecular basis for the conversion of this robust monomeric protein into an amyloid-competent state. | ||
| - | + | A regulatable switch mediates self-association in an immunoglobulin fold.,Calabrese MF, Eakin CM, Wang JM, Miranker AD Nat Struct Mol Biol. 2008 Sep;15(9):965-71. PMID:19172750<ref>PMID:19172750</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3ciq" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Human]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Calabrese, M F]] | |
| - | == | + | [[Category: Eakin, C M]] |
| - | + | [[Category: Miranker, A D]] | |
| - | + | [[Category: Wang, J M]] | |
| - | + | ||
| - | < | + | |
| - | [[Category: | + | |
| - | [[Category: Calabrese, M F | + | |
| - | [[Category: Eakin, C M | + | |
| - | [[Category: Miranker, A D | + | |
| - | [[Category: Wang, J M | + | |
[[Category: Amyloid]] | [[Category: Amyloid]] | ||
[[Category: Beta-2 microglobulin]] | [[Category: Beta-2 microglobulin]] | ||
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[[Category: Pyrrolidone carboxylic acid]] | [[Category: Pyrrolidone carboxylic acid]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 25 10:07:08 2009'' | ||
Current revision
A regulatable switch mediates self-association in an immunoglobulin fold
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Categories: Human | Large Structures | Calabrese, M F | Eakin, C M | Miranker, A D | Wang, J M | Amyloid | Beta-2 microglobulin | Class-1 mhc | Dialysis-related amyloidosis | Disease mutation | Glycation | Glycoprotein | Immune response | Immune system | Immunoglobulin domain | Mhc i | Protein folding | Pyrrolidone carboxylic acid | Secreted

