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3tfk

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Current revision (13:26, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tfk' size='340' side='right'caption='[[3tfk]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='3tfk' size='340' side='right'caption='[[3tfk]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tfk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tfk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFK FirstGlance]. <br>
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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=NO3:NITRATE+ION'>NO3</scene></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]] 2.753&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oi9|2oi9]], [[3tf7|3tf7]], [[3tjh|3tjh]], [[3tpu|3tpu]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=3tfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfk OCA], [https://pdbe.org/3tfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfk RCSB], [https://www.ebi.ac.uk/pdbsum/3tfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfk 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=3tfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfk OCA], [https://pdbe.org/3tfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfk RCSB], [https://www.ebi.ac.uk/pdbsum/3tfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfk ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_MOUSE] Involved in the presentation of foreign antigens to the immune system.
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T cell receptor (TCR) engagement of peptide-major histocompatibility complex (pMHC) is essential to adaptive immunity, but it is unknown whether TCR signaling responses are influenced by the binding topology of the TCR-peptide-MHC complex. We developed yeast-displayed pMHC libraries that enabled us to identify new peptide sequences reactive with a single TCR. Structural analysis showed that four peptides bound to the TCR with distinct 3D and 2D affinities using entirely different binding chemistries. Three of the peptides that shared a common docking mode, where key TCR-MHC germline interactions are preserved, induced TCR signaling. The fourth peptide failed to induce signaling and was recognized in a substantially different TCR-MHC binding mode that apparently exceeded geometric tolerances compatible with signaling. We suggest that the stereotypical TCR-MHC docking paradigm evolved from productive signaling geometries and that TCR signaling can be modulated by peptides that are recognized in alternative TCR-pMHC binding orientations.
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T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex.,Adams JJ, Narayanan S, Liu B, Birnbaum ME, Kruse AC, Bowerman NA, Chen W, Levin AM, Connolly JM, Zhu C, Kranz DM, Garcia KC Immunity. 2011 Nov 16. PMID:22101157<ref>PMID:22101157</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 3tfk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Adams, J J]]
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[[Category: Adams JJ]]
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[[Category: Garcia, K C]]
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[[Category: Garcia KC]]
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[[Category: Kranz, D M]]
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[[Category: Kranz DM]]
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[[Category: Antigen recognition]]
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[[Category: Chimera protein]]
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[[Category: Ig mhc]]
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[[Category: Immune system]]
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[[Category: Membrane receptor]]
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[[Category: Tcr-pmhc]]
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Current revision

42F3-p4B10/H2-Ld

PDB ID 3tfk

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