3na4

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[[Image:3na4.jpg|left|200px]]
 
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==D53P beta-2 microglobulin mutant==
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The line below this paragraph, containing "STRUCTURE_3na4", creates the "Structure Box" on the page.
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<StructureSection load='3na4' size='340' side='right'caption='[[3na4]], [[Resolution|resolution]] 1.90&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'>[[3na4]] 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=3NA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NA4 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]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene></td></tr>
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{{STRUCTURE_3na4| PDB=3na4 | SCENE= }}
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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=3na4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3na4 OCA], [https://pdbe.org/3na4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3na4 RCSB], [https://www.ebi.ac.uk/pdbsum/3na4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3na4 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Proteins hosting main beta-sheets adopt specific strategies to avoid intermolecular interactions leading to aggregation and amyloid deposition. Human beta-2 microglobulin (beta2m) displays a typical immunoglobulin fold and is known to be amyloidogenic in vivo. Upon severe kidney deficiency beta2m accumulates in the blood stream, triggering, over the years, pathologic deposition of large amyloid aggregates in joints and bones. A beta-bulge observed on the edge D beta-strand of some beta2m crystal structures has been suggested to be crucial in protecting the protein from amyloid aggregation. Conversely, a straight D-strand, observed in different crystal structures of monomeric beta2m, would promote amyloid aggregation. More recently, the different conformations observed for beta2m D-strand have been interpreted as the result of intrinsic flexibility rather than assigned to a functional protective role against aggregation. To shed light on such contrasting picture, the mutation Asp53--&gt;Pro was engineered in beta2m, in order to impair the formation of a regular/straight D-strand. Such mutant was characterised structurally and biophysically, by means of circular dichroism, X-ray crystallography and mass spectrometry, additionally assessing its amyloid aggregation trends in vitro. The results here presented highlight the conformational plasticity of the edge D-strand, and show that even perturbing the D-strand structure through a Pro residue has only marginal effects in protecting beta2m from amyloid aggregation in vitro.
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===D53P beta-2 microglobulin mutant===
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D-strand perturbation and amyloid propensity in Beta-2 microglobulin.,Azinas S, Colombo M, Barbiroli A, Santambrogio C, Giorgetti S, Raimondi S, Bonomi F, Grandori R, Bellotti V, Ricagno S, Bolognesi M FEBS J. 2011 May 13. doi: 10.1111/j.1742-4658.2011.08157.x. PMID:21569201<ref>PMID:21569201</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 3na4" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21569201}}, 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 21569201 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21569201}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3na4]] is a 1 chain structure with 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=3NA4 OCA].
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==Reference==
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<ref group="xtra">PMID:021569201</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Azinas, S.]]
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[[Category: Large Structures]]
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[[Category: Bolognesi, M.]]
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[[Category: Azinas S]]
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[[Category: Ricagno, S.]]
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[[Category: Bolognesi M]]
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[[Category: Ricagno S]]

Current revision

D53P beta-2 microglobulin mutant

PDB ID 3na4

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