2z9t

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[[Image:2z9t.jpg|left|200px]]
 
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==Crystal structure of the human beta-2 microglobulin mutant W60G==
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The line below this paragraph, containing "STRUCTURE_2z9t", creates the "Structure Box" on the page.
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<StructureSection load='2z9t' size='340' side='right'caption='[[2z9t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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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'>[[2z9t]] 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=2Z9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z9T 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]] 1.8&#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=2z9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z9t OCA], [https://pdbe.org/2z9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z9t RCSB], [https://www.ebi.ac.uk/pdbsum/2z9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z9t ProSAT]</span></td></tr>
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{{STRUCTURE_2z9t| PDB=2z9t | SCENE= }}
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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/z9/2z9t_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=2z9t 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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'''Crystal structure of the human beta-2 microglobulin mutant W60G'''
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2Z9T is a [[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=2Z9T OCA].
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</div>
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<div class="pdbe-citations 2z9t" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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):885-95. Epub 2008 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18395224 18395224]
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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>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bellotti, V.]]
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[[Category: Bellotti V]]
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[[Category: Betto, E.]]
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[[Category: Betto E]]
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[[Category: Bolognesi, B.]]
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[[Category: Bolognesi B]]
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[[Category: Bolognesi, M.]]
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[[Category: Bolognesi M]]
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[[Category: Corazza, A.]]
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[[Category: Corazza A]]
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[[Category: Fogolari, F.]]
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[[Category: Fogolari F]]
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[[Category: Giorgetti, S.]]
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[[Category: Giorgetti S]]
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[[Category: Gural, D.]]
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[[Category: Gural D]]
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[[Category: Merlini, G.]]
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[[Category: Merlini G]]
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[[Category: Mimmi, M C.]]
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[[Category: Mimmi MC]]
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[[Category: Pucillo, C.]]
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[[Category: Pucillo C]]
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[[Category: Raimondi, S.]]
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[[Category: Raimondi S]]
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[[Category: Rennella, E.]]
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[[Category: Rennella E]]
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[[Category: Ricagno, S.]]
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[[Category: Ricagno S]]
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[[Category: Stoppini, M.]]
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[[Category: Stoppini M]]
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[[Category: Viglino, P.]]
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[[Category: Viglino P]]
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[[Category: Amyloidosis]]
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[[Category: Beta fibril]]
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[[Category: Beta-2-microglobulin]]
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[[Category: Disease mutation]]
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[[Category: Dra]]
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[[Category: Glycation]]
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[[Category: Glycine]]
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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 domain]]
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[[Category: Mhc i]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Secreted]]
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[[Category: Tryptophan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:45:02 2008''
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Current revision

Crystal structure of the human beta-2 microglobulin mutant W60G

PDB ID 2z9t

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