2ol3

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[[Image:2ol3.gif|left|200px]]<br /><applet load="2ol3" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ol3, resolution 2.90&Aring;" />
 
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'''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule'''<br />
 
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==Overview==
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==crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule==
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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.
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<StructureSection load='2ol3' size='340' side='right'caption='[[2ol3]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.9&#8491;</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q5R1F1_MOUSE Q5R1F1_MOUSE]
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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/ol/2ol3_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=2ol3 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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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.
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==About this Structure==
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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>
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2OL3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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 Mar 15;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17363906 17363906]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 2ol3" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Auphan-Anezin, N.]]
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[[Category: Gregoire, C.]]
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[[Category: Guimezanes, A.]]
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[[Category: Kearney, A.]]
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[[Category: Kellenberger, C.]]
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[[Category: Malissen, B.]]
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[[Category: Mazza, C.]]
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[[Category: Merwe, P.A.Van.der.]]
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[[Category: Roussel, A.]]
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[[Category: Schmitt-Verhulst, A.M.]]
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[[Category: NAG]]
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[[Category: class i mhc]]
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[[Category: h-2kbm8]]
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[[Category: t cell receptor]]
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[[Category: tcr-pmhc complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:32:35 2008''
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==See Also==
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Auphan-Anezin N]]
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[[Category: Gregoire C]]
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[[Category: Guimezanes A]]
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[[Category: Kearney A]]
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[[Category: Kellenberger C]]
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[[Category: Malissen B]]
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[[Category: Mazza C]]
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[[Category: Roussel A]]
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[[Category: Schmitt-Verhulst AM]]
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[[Category: Van der Merwe PA]]

Current revision

crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule

PDB ID 2ol3

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