9uvi

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m (Protected "9uvi" [edit=sysop:move=sysop])
Current revision (10:52, 3 September 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9uvi is ON HOLD until Paper Publication
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==Crystal structure of beta 2 microglobulin in complex with antibody BBM.1==
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<StructureSection load='9uvi' size='340' side='right'caption='[[9uvi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9uvi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UVI 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]] 2.5&#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=9uvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9uvi OCA], [https://pdbe.org/9uvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9uvi RCSB], [https://www.ebi.ac.uk/pdbsum/9uvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9uvi 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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beta(2)-Microglobulin (beta(2)M) is an essential component of major histocompatibility complex class I (MHC-I) molecules, with a well established canonical role in immune surveillance. Beyond its classical functions, accumulating evidence has highlighted beta(2)M as a multifaceted biomarker, with elevated serum levels closely associated with disease burden and prognosis in metabolic disorders, malignancies, autoimmune diseases and central nervous system conditions. In this study, we resolved the crystal structure of human beta(2)M in complex with the mouse monoclonal antibody BBM.1 at 2.50 A resolution using X-ray crystallography. Structural analysis revealed that BBM.1 binds beta(2)M through multiple CDRs, recognizing key surface residues including Glu36, Asp38, Lys41, Asn42, Glu44, Arg45, Glu47 and Arg81. The interaction is anchored by a central hydrophobic core formed by Trp32 (light chain), Trp99 (heavy chain) and Ile92 (beta(2)M), which is deeply buried in the interface. Surrounding this core is a well organized polar interaction network composed of hydrogen bonds and salt bridges, primarily involving beta(2)M residues Lys41, Glu44, Arg45 and Glu47. Notably, the Arg45 residue deeply embeds into the antibody-binding pocket, forming several crucial interactions. These findings not only validate previous biochemical and mutational data but also identify new epitope residues, providing a structural foundation for the development and optimization of precision therapeutic strategies targeting beta(2)M.
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Authors:
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Crystal structure of the beta(2)-microglobulin-BBM.1 antibody complex reveals the molecular basis of antigen recognition.,Wu J, Zeng F, Wang X, Wei P Acta Crystallogr D Struct Biol. 2025 Sep 1;81(Pt 9):473-481. doi: , 10.1107/S2059798325006370. Epub 2025 Aug 1. PMID:40748259<ref>PMID:40748259</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9uvi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Wei PC]]
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[[Category: Wu JJ]]

Current revision

Crystal structure of beta 2 microglobulin in complex with antibody BBM.1

PDB ID 9uvi

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