2vll

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[[Image:2vll.png|left|200px]]
 
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{{STRUCTURE_2vll| PDB=2vll | SCENE= }}
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==The Structural Dynamics and Energetics of an Immunodominant T-cell Receptor are Programmed by its Vbeta Domain==
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<StructureSection load='2vll' size='340' side='right'caption='[[2vll]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vll]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VLL 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]] 1.6&#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=2vll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vll OCA], [https://pdbe.org/2vll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vll RCSB], [https://www.ebi.ac.uk/pdbsum/2vll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vll ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/M1_I34A1 M1_I34A1] Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.<ref>PMID:11531417</ref> Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.<ref>PMID:11531417</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/vl/2vll_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vll 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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Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A*0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype.
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===THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN IMMUNODOMINANT T-CELL RECEPTOR ARE PROGRAMMED BY ITS VBETA DOMAIN===
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The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain.,Ishizuka J, Stewart-Jones GB, van der Merwe A, Bell JI, McMichael AJ, Jones EY Immunity. 2008 Feb;28(2):171-82. PMID:18275829<ref>PMID:18275829</ref>
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{{ABSTRACT_PUBMED_18275829}}
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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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==About this Structure==
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<div class="pdbe-citations 2vll" style="background-color:#fffaf0;"></div>
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[[2vll]] is a 6 chain structure of [[Beta-2 microglobulin]] and [[Major histocompatibility complex]] 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=2VLL OCA].
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==See Also==
==See Also==
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*[[Beta-2 microglobulin|Beta-2 microglobulin]]
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[Major histocompatibility complex|Major histocompatibility complex]]
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*[[MHC 3D structures|MHC 3D structures]]
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*[[MHC I 3D structures|MHC I 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:018275829</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bell, J.]]
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[[Category: Large Structures]]
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[[Category: Ishizuka, J.]]
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[[Category: Unidentified influenza virus]]
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[[Category: Jones, Y.]]
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[[Category: Bell J]]
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[[Category: Mcmichael, A.]]
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[[Category: Ishizuka J]]
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[[Category: Merwe, A Van Der.]]
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[[Category: Jones Y]]
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[[Category: Stewart-Jones, G.]]
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[[Category: Mcmichael A]]
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[[Category: Complex]]
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[[Category: Stewart-Jones G]]
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[[Category: Disease mutation]]
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[[Category: Van Der Merwe A]]
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[[Category: Flu]]
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[[Category: Glycation]]
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[[Category: Glycoprotein]]
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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: Immune system-receptor-complex]]
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[[Category: Immunodominance]]
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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: Pyrrolidone carboxylic acid]]
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[[Category: Receptor]]
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[[Category: Secreted]]
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[[Category: T-cell]]
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[[Category: Tcr]]
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[[Category: Transmembrane]]
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Current revision

The Structural Dynamics and Energetics of an Immunodominant T-cell Receptor are Programmed by its Vbeta Domain

PDB ID 2vll

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