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3ox8

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Current revision (11:19, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3ox8' size='340' side='right'caption='[[3ox8]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='3ox8' size='340' side='right'caption='[[3ox8]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ox8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ox8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX8 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oxr|3oxr]], [[3oxs|3oxs]]</div></td></tr>
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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]] 2.16&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-A, MHC HLA-A*02:03 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), B2M, BETA 2-MICROGLOBULIN, CDABP0092, HDCMA22P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ox8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox8 OCA], [https://pdbe.org/3ox8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox8 ProSAT]</span></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=3ox8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox8 OCA], [https://pdbe.org/3ox8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox8 ProSAT]</span></td></tr>
</table>
</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>
 
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q2LC95_HUMAN Q2LC95_HUMAN]] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364] [[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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[https://www.uniprot.org/uniprot/Q2LC95_HUMAN Q2LC95_HUMAN] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Binding of specific antigenic peptides with human leukocyte antigen (HLA) molecules is a prerequisite for the initiation of T-cell responses and structural information about the peptide-HLA complex is essential for the detailed understanding of such interactions. HLA-A2 is the most prevalent HLA allele globally but aside from A*02:01 there is a significant lack of crystal structures, particularly for alleles that occur in high frequencies among Asian populations. Here, we report three HLA-A2 structures with the immunodominant hepatitis B core antigen 18-27 (HBcAg18-27) epitope, namely A*02:03, A*02:06, and A*02:07 at resolutions of 2.16, 1.70, and 1.75 A respectively. This comparative analysis reveals that minor polymorphic residue changes between different HLA alleles can induce significant alterations in the major histocompatibility complex-peptide interface, and introduce conformational changes in the p3-p8 peptide region. Circular dichroism analysis demonstrated the HLA-A2-peptide complexes to have a hierarchy of thermostability and binding affinity in the order of A*02:06&gt;A*02:07&gt;A*02:01&gt;A*02:03. Our findings provide structural insights into the varied HLA-A2 allele binding of the hepatitis B core antigen 18-27 epitope and the data suggest that chemical modifications of the peptide side chains could be a promising strategy to modulate and improve HLA-A2-peptide binding affinity for vaccine design.
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Structural insights into the binding of hepatitis B virus core peptide to HLA-A2 alleles: Towards designing better vaccines.,Liu J, Chen KY, Ren EC Eur J Immunol. 2011 Jul;41(7):2097-106. doi: 10.1002/eji.201041370. PMID:21538979<ref>PMID:21538979</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 3ox8" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[MHC 3D structures|MHC 3D structures]]
 
*[[Major histocompatibility complex|Major histocompatibility complex]]
*[[Major histocompatibility complex|Major histocompatibility complex]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Hepatitis B virus]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Y]]
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[[Category: Chen Y]]
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[[Category: Lai, L]]
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[[Category: Lai L]]
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[[Category: Liu, J]]
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[[Category: Liu J]]
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[[Category: Ren, E]]
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[[Category: Ren E]]
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[[Category: Antigen presentation]]
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[[Category: Beta-sheet]]
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[[Category: Cell surface]]
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[[Category: Helix]]
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[[Category: Host-virus interaction]]
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[[Category: Immune system]]
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[[Category: Immunogenicity]]
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[[Category: Peptide binding]]
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[[Category: Protein-peptide complex]]
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[[Category: Tcr recognition]]
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[[Category: Therapeutic design]]
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Current revision

Crystal Structure of HLA A*02:03 Bound to HBV Core 18-27

PDB ID 3ox8

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