2vb5

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{{Seed}}
 
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[[Image:2vb5.png|left|200px]]
 
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==Solution structure of W60G mutant of human beta2-microglobulin==
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The line below this paragraph, containing "STRUCTURE_2vb5", creates the "Structure Box" on the page.
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<StructureSection load='2vb5' size='340' side='right'caption='[[2vb5]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vb5]] 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=2VB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VB5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=2vb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb5 OCA], [https://pdbe.org/2vb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vb5 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2vb5| PDB=2vb5 | SCENE= }}
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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/vb/2vb5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2vb5 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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Amyloidosis associated to hemodialysis is caused by persistently high beta(2)-microglobulin (beta(2)m) serum levels. beta(2)m is an intrinsically amyloidogenic protein whose capacity to assemble into amyloid fibrils in vitro and in vivo is concentration dependent; no beta(2)m genetic variant is known in the human population. We investigated the roles of two evolutionary conserved Trp residues in relation to beta(2)m structure, function and folding/misfolding by means of a combined biophysical and functional approach. We show that Trp60 plays a functional role in promoting the association of beta(2)m in class I major histocompatibility complex; it is exposed to the solvent at the apex of a protein loop in order to accomplish such function. The Trp60--&gt;Gly mutation has a threefold effect: it stabilizes beta(2)m, inhibits beta(2)m amyloidogenic propensity and weakens the interaction with the class I major histocompatibility complex heavy chain. On the contrary, Trp95 is buried in the beta(2)m core; the Trp95--&gt;Gly mutation destabilizes the protein, which is unfolded in solution, yielding nonfibrillar beta(2)m aggregates. Trp60 and Trp95 therefore play differential and complementary roles in beta(2)m, being relevant for function (Trp60) and for maintenance of a properly folded structure (Trp95) while affecting in distinct ways the intrinsic propensity of wild-type beta(2)m towards self-aggregation into amyloid fibrils.
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===SOLUTION STRUCTURE OF W60G MUTANT OF HUMAN BETA2-MICROGLOBULIN===
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The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties.,Esposito G, Ricagno S, Corazza A, Rennella E, Gumral D, Mimmi MC, Betto E, Pucillo CE, Fogolari F, Viglino P, Raimondi S, Giorgetti S, Bolognesi B, Merlini G, Stoppini M, Bolognesi M, Bellotti V J Mol Biol. 2008 May 9;378(4):887-97. Epub 2008 Mar 8. PMID:18395224<ref>PMID:18395224</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2vb5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18395224}}, adds the Publication Abstract to the page
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18395224 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18395224}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2VB5 is a 1 chain 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=2VB5 OCA].
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==Reference==
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<ref group="xtra">PMID:18395224</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bellotti, V.]]
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[[Category: Large Structures]]
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[[Category: Bolognesi, B.]]
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[[Category: Bellotti V]]
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[[Category: Corazza, A.]]
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[[Category: Bolognesi B]]
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[[Category: Esposito, G.]]
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[[Category: Corazza A]]
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[[Category: Fogolari, F.]]
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[[Category: Esposito G]]
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[[Category: Giorgetti, S.]]
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[[Category: Fogolari F]]
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[[Category: Gumral, D.]]
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[[Category: Giorgetti S]]
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[[Category: Merlini, G.]]
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[[Category: Gumral D]]
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[[Category: Mimmi, M C.]]
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[[Category: Merlini G]]
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[[Category: Raimondi, S.]]
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[[Category: Mimmi MC]]
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[[Category: Rennella, E.]]
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[[Category: Raimondi S]]
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[[Category: Stoppini, M.]]
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[[Category: Rennella E]]
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[[Category: Viglino, P.]]
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[[Category: Stoppini M]]
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[[Category: Amyloid disease]]
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[[Category: Viglino P]]
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[[Category: Glycation]]
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[[Category: Glycoprotein]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin constant domain]]
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[[Category: Immunoglobulin domain]]
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[[Category: Mhc i]]
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[[Category: Secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:54:07 2009''
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Current revision

Solution structure of W60G mutant of human beta2-microglobulin

PDB ID 2vb5

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