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| | <StructureSection load='3bvn' size='340' side='right'caption='[[3bvn]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='3bvn' size='340' side='right'caption='[[3bvn]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bvn]] 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=3BVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BVN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bvn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BVN FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uxs|1uxs]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), B2M ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3bvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bvn OCA], [https://pdbe.org/3bvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bvn RCSB], [https://www.ebi.ac.uk/pdbsum/3bvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bvn 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=3bvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bvn OCA], [https://pdbe.org/3bvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bvn RCSB], [https://www.ebi.ac.uk/pdbsum/3bvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bvn ProSAT]</span></td></tr> |
| | </table> | | </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 == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LMP2_EBVB9 LMP2_EBVB9]] Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs.<ref>PMID:8290598</ref> <ref>PMID:9768760</ref> Isoform LMP2B may be a negative regulator of isoform LMP2A.<ref>PMID:8290598</ref> <ref>PMID:9768760</ref> [[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.
| + | [https://www.uniprot.org/uniprot/Q56H30_HUMAN Q56H30_HUMAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
| | *[[MHC 3D structures|MHC 3D structures]] | | *[[MHC 3D structures|MHC 3D structures]] |
| | + | *[[MHC I 3D structures|MHC I 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | + | [[Category: Human herpesvirus 4 strain B95-8]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kumar, P]] | + | [[Category: Kumar P]] |
| - | [[Category: Saenger, W]] | + | [[Category: Saenger W]] |
| - | [[Category: Uchanska-Ziegler, B]] | + | [[Category: Uchanska-Ziegler B]] |
| - | [[Category: Vahedi-Faridi, A]] | + | [[Category: Vahedi-Faridi A]] |
| - | [[Category: Ziegler, A]] | + | [[Category: Ziegler A]] |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Ankylosing spondylitis]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Glycation]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hla]]
| + | |
| - | [[Category: Hla-b*14]]
| + | |
| - | [[Category: Hla-b*1402]]
| + | |
| - | [[Category: Hla-b14]]
| + | |
| - | [[Category: Hla-b1402]]
| + | |
| - | [[Category: Host-virus interaction]]
| + | |
| - | [[Category: Human leukocyte antigen]]
| + | |
| - | [[Category: Immune response]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Major histocompatibility complex]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Mhc]]
| + | |
| - | [[Category: Mhc i]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Plmp2]]
| + | |
| - | [[Category: Pyrrolidone carboxylic acid]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Ubl conjugation]]
| + | |
| Structural highlights
Function
Q56H30_HUMAN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The existence of cytotoxic T cells (CTL) cross-reacting with the human major histocompatibility antigens HLA-B14 and HLA-B27 suggests that their alloreactivity could be due to presentation of shared peptides in similar binding modes by these molecules. We therefore determined the crystal structures of the subtypes HLA-B*1402, HLA-B*2705, and HLA-B*2709 in complex with a proven self-ligand, pCatA (peptide with the sequence IRAAPPPLF derived from cathepsin A (residues 2-10)), and of HLA-B*1402 in complex with a viral peptide, pLMP2 (RRRWRRLTV, derived from latent membrane protein 2 (residues 236-244) of Epstein-Barr virus). Despite the exchange of 18 residues within the binding grooves of HLA-B*1402 and HLA-B*2705 or HLA-B*2709, the pCatA peptide is presented in nearly identical conformations. However, pLMP2 is displayed by HLA-B*1402 in a conformation distinct from those previously found in the two HLA-B27 subtypes. In addition, the complexes of HLA-B*1402 with the two peptides reveal a nonstandard, tetragonal mode of the peptide N terminus anchoring in the binding groove because of the exchange of the common Tyr-171 by His-171 of the HLA-B*1402 heavy chain. This exchange appears also responsible for reduced stability of HLA-B14-peptide complexes in vivo and slow assembly in vitro. The studies with the pCatA peptide uncover that CTL cross-reactive between HLA-B14 and HLA-B27 might primarily recognize the common structural features of the bound peptide, thus neglecting amino acid replacements within the rim of the binding grooves. In contrast, structural alterations between the three complexes with the pLMP2 peptide indicate how heavy chain polymorphisms can influence peptide display and prevent CTL cross-reactivity between HLA-B14 and HLA-B27 antigens.
Structural basis for T cell alloreactivity among three HLA-B14 and HLA-B27 antigens.,Kumar P, Vahedi-Faridi A, Saenger W, Merino E, Lopez de Castro JA, Uchanska-Ziegler B, Ziegler A J Biol Chem. 2009 Oct 23;284(43):29784-97. Epub 2009 Jul 18. PMID:19617632[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kumar P, Vahedi-Faridi A, Saenger W, Merino E, Lopez de Castro JA, Uchanska-Ziegler B, Ziegler A. Structural basis for T cell alloreactivity among three HLA-B14 and HLA-B27 antigens. J Biol Chem. 2009 Oct 23;284(43):29784-97. Epub 2009 Jul 18. PMID:19617632 doi:10.1074/jbc.M109.038497
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