3oxr: Difference between revisions

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-{{STRUCTURE_3oxr|  PDB=3oxr  |  SCENE=  }}
-===Crystal Structure of HLA A*02:06 Bound to HBV Core 18-27===
-{{ABSTRACT_PUBMED_21538979}}
-==Disease==
+==Crystal Structure of HLA A*02:06 Bound to HBV Core 18-27==
-[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://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>
+<StructureSection load='3oxr' size='340' side='right'caption='[[3oxr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3oxr]] is a 3 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=3OXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OXR 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]] 1.7&#8491;</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=3oxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxr OCA], [https://pdbe.org/3oxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oxr RCSB], [https://www.ebi.ac.uk/pdbsum/3oxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q5MAG5_HUMAN Q5MAG5_HUMAN] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Function==
+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>
-[[http://www.uniprot.org/uniprot/Q5MAG5_HUMAN Q5MAG5_HUMAN]] Involved in the presentation of foreign antigens to the immune system (By similarity).[SAAS:SAAS003006_004_004364] [[http://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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[3oxr]] is a 3 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=3OXR OCA].
+</div>
+<div class="pdbe-citations 3oxr" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Beta-2 microglobulin|Beta-2 microglobulin]]
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
-*[[Major histocompatibility complex|Major histocompatibility complex]]
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:021538979</ref><references group="xtra"/><references/>
+</StructureSection>
+[[Category: Hepatitis B virus]]
 [[Category: Homo sapiens]]
-[[Category: Chen, Y.]]
+[[Category: Large Structures]]
-[[Category: Lai, L.]]
+[[Category: Chen Y]]
-[[Category: Liu, J.]]
+[[Category: Lai L]]
-[[Category: Ren, E.]]
+[[Category: Liu J]]
-[[Category: Antigen presentation]]
+[[Category: Ren E]]
-[[Category: Beta-sheet]]
-[[Category: Cell surface]]
-[[Category: Helix]]
-[[Category: Host-virus interaction]]
-[[Category: Immune system]]
-[[Category: Immunogenicity]]
-[[Category: Peptide binding]]
-[[Category: Protein-peptide complex]]
-[[Category: Tcr recognition]]
-[[Category: Therapeutic design]]