5ib5: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ib5 is ON HOLD
+==Crystal structure of HLA-B*27:09 complexed with the self-peptide pVIPR and Copper==
+<StructureSection load='5ib5' size='340' side='right'caption='[[5ib5]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ib5]] is a 6 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=5IB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IB5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5ib5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ib5 OCA], [https://pdbe.org/5ib5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ib5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ib5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ib5 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.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Conformational changes of major histocompatibility complex (MHC) antigens have the potential to be recognized by T cells and may arise from polymorphic variation of the MHC molecule, the binding of modifying ligands, or both. Here, we investigated whether metal ions could affect allele-dependent structural variation of the two minimally distinct human leukocyte antigen (HLA)-B*27:05 and HLA-B*27:09 subtypes, which exhibit differential association with the rheumatic disease ankylosing spondylitis (AS). We employed NMR spectroscopy and X-ray crystallography coupled with ensemble refinement to study the AS-associated HLA-B*27:05 subtype and the AS non-associated HLA-B* 27:09 in complex with the self-peptide pVIPR (RRKWRRWHL). Both techniques revealed that pVIPR exhibits a higher degree of flexibility when complexed with HLA-B* 27:05 than with HLA-B*27:09. Furthermore, we found that the binding of the metal ions Cu2+ or Ni2+, but not Mn2+, Zn2+, or Hg2+ affects the structure of a pVIPR-bound HLA-B*27 molecule in a subtype-dependent manner. In HLA-B*27:05, the metals triggered conformational reorientations of pVIPR, but no such structural changes were observed in the HLA-B*27:09 subtype, with or without bound metal ion. These observations provide the first demonstration that not only MHC class II, but also class I molecules can undergo metal ion-induced conformational alterations. Our findings suggest that metals may have role in triggering rheumatic diseases such as AS and also have implications for the molecular basis of metal-induced hypersensitivities and allergies.
-Authors: Janke, R., Ballaschk, M., Schmieder, P., Uchanska-Ziegler, B., Ziegler, A., Loll, B.
+Metal-triggered conformational reorientation of a self-peptide bound to a disease-associated HLA-B*27 subtype.,Driller R, Ballaschk M, Schmieder P, Uchanska-Ziegler B, Ziegler A, Loll B J Biol Chem. 2019 Jul 11. pii: RA119.008937. doi: 10.1074/jbc.RA119.008937. PMID:31296658<ref>PMID:31296658</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Ballaschk, M]]
+<div class="pdbe-citations 5ib5" style="background-color:#fffaf0;"></div>
-[[Category: Schmieder, P]]
-[[Category: Janke, R]]
+==See Also==
-[[Category: Uchanska-Ziegler, B]]
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
-[[Category: Loll, B]]
+== References ==
-[[Category: Ziegler, A]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Ballaschk M]]
+[[Category: Janke R]]
+[[Category: Loll B]]
+[[Category: Schmieder P]]
+[[Category: Uchanska-Ziegler B]]
+[[Category: Ziegler A]]