2ol3: Difference between revisions
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==crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule== | |||
<StructureSection load='2ol3' size='340' side='right'caption='[[2ol3]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ol3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OL3 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2ol3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol3 OCA], [https://pdbe.org/2ol3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ol3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ol3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ol3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5R1F1_MOUSE Q5R1F1_MOUSE] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/2ol3_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2ol3 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Binding degeneracy is thought to constitute a fundamental property of the T-cell antigen receptor (TCR), yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and a peptide (pBM8) bound to the H-2K(bm8) major histocompatibility complex (MHC) molecule, and compared it with the structures of the BM3.3 TCR bound to H-2K(b) molecules loaded with two peptides that had a minimal level of primary sequence identity with pBM8. Our findings provide a refined structural view of the basis of BM3.3 TCR cross-reactivity and a structural explanation for the long-standing paradox that a TCR antigen-binding site can be both specific and degenerate. We also measured the thermodynamic features and biological penalties that incurred during cross-recognition. Our data illustrate the difficulty for a given TCR in adapting to distinct peptide-MHC surfaces while still maintaining affinities that result in functional in vivo responses. Therefore, when induction of protective effector T cells is used as the ultimate criteria for adaptive immunity, TCRs are probably much less degenerate than initially assumed. | |||
How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?,Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, Roussel A, Kearney A, van der Merwe PA, Schmitt-Verhulst AM, Malissen B EMBO J. 2007 Apr 4;26(7):1972-83. Epub 2007 Mar 15. PMID:17363906<ref>PMID:17363906</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ol3" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Auphan-Anezin N]] | |||
[[Category: Auphan-Anezin | [[Category: Gregoire C]] | ||
[[Category: Gregoire | [[Category: Guimezanes A]] | ||
[[Category: Guimezanes | [[Category: Kearney A]] | ||
[[Category: Kearney | [[Category: Kellenberger C]] | ||
[[Category: Kellenberger | [[Category: Malissen B]] | ||
[[Category: Malissen | [[Category: Mazza C]] | ||
[[Category: Mazza | [[Category: Roussel A]] | ||
[[Category: Schmitt-Verhulst AM]] | |||
[[Category: Roussel | [[Category: Van der Merwe PA]] | ||
[[Category: Schmitt-Verhulst | |||
[[Category: | |||
Latest revision as of 08:24, 30 October 2024
crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule
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