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3kxf

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[[Image:3kxf.png|left|200px]]
 
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==Crystal Structure of SB27 TCR in complex with the 'restriction triad' mutant HLA-B*3508-13mer==
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The line below this paragraph, containing "STRUCTURE_3kxf", creates the "Structure Box" on the page.
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<StructureSection load='3kxf' size='340' side='right'caption='[[3kxf]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3kxf]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KXF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3KXF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kww|3kww]], [[2ak4|2ak4]]</td></tr>
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{{STRUCTURE_3kxf| PDB=3kxf | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3kxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kxf OCA], [http://pdbe.org/3kxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kxf RCSB], [http://www.ebi.ac.uk/pdbsum/3kxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kxf ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[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>
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== Function ==
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[[http://www.uniprot.org/uniprot/1B35_HUMAN 1B35_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[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. [[http://www.uniprot.org/uniprot/BZLF1_EBVB9 BZLF1_EBVB9]] Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).<ref>PMID:2157874</ref> <ref>PMID:1847997</ref> <ref>PMID:8404860</ref> <ref>PMID:17079287</ref> <ref>PMID:19144704</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kxf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kxf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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alphabeta T cell receptors (TCRs) are genetically restricted to corecognize peptide antigens bound to self-major histocompatibility complex (pMHC) molecules; however, the basis for this MHC specificity remains unclear. Despite the current dogma, evaluation of the TCR-pMHC-I structural database shows that the nongermline-encoded complementarity-determining region (CDR)-3 loops often contact the MHC-I, and the germline-encoded CDR1 and -2 loops frequently participate in peptide-mediated interactions. Nevertheless, different TCRs adopt a roughly conserved docking mode over the pMHC-I, in which three MHC-I residues (65, 69, and 155) are invariably contacted by the TCR in one way or another. Nonetheless, the impact of mutations at these three positions, either individually or together, was not uniformly detrimental to TCR recognition of pHLA-B*0801 or pHLA-B*3508. Moreover, when TCR-pMHC-I recognition was impaired, this could be partially restored by expression of the CD8 coreceptor. The structure of a TCR-pMHC-I complex in which these three (65, 69, and 155) MHC-I positions were all mutated resulted in shifting of the TCR footprint relative to the cognate complex and formation of compensatory interactions. Collectively, our findings reveal the inherent adaptability of the TCR in maintaining peptide recognition while accommodating changes to the central docking site on the pMHC-I.
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===Crystal Structure of SB27 TCR in complex with the 'restriction triad' mutant HLA-B*3508-13mer===
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Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability.,Burrows SR, Chen Z, Archbold JK, Tynan FE, Beddoe T, Kjer-Nielsen L, Miles JJ, Khanna R, Moss DJ, Liu YC, Gras S, Kostenko L, Brennan RM, Clements CS, Brooks AG, Purcell AW, McCluskey J, Rossjohn J Proc Natl Acad Sci U S A. 2010 May 18. PMID:20483993<ref>PMID:20483993</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 3kxf" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20483993}}, adds the Publication Abstract to the page
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20483993 is the PubMed ID number.
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*[[MHC 3D structures|MHC 3D structures]]
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*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
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{{ABSTRACT_PUBMED_20483993}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3kxf]] is a 20 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=3KXF OCA].
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</StructureSection>
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[[Category: Human]]
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==Reference==
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[[Category: Large Structures]]
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<ref group="xtra">PMID:20483993</ref><references group="xtra"/>
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[[Category: Archbold, J K]]
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[[Category: Homo sapiens]]
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[[Category: Gras, S]]
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[[Category: Archbold, J K.]]
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[[Category: Rossjohn, J]]
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[[Category: Gras, S.]]
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[[Category: Tynan, F E]]
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[[Category: Rossjohn, J.]]
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[[Category: Disulfide bond]]
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[[Category: Tynan, F E.]]
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[[Category: Hla]]
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[[Category: Host-virus interaction]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin domain]]
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[[Category: Membrane]]
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[[Category: Mhc]]
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[[Category: Mhc i]]
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[[Category: Tcr]]
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[[Category: Transmembrane]]

Current revision

Crystal Structure of SB27 TCR in complex with the 'restriction triad' mutant HLA-B*3508-13mer

PDB ID 3kxf

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