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1fng

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(New page: 200px<br /><applet load="1fng" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fng, resolution 1.90&Aring;" /> '''HISTOCOMPATIBILITY A...)
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[[Image:1fng.gif|left|200px]]<br /><applet load="1fng" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fng, resolution 1.90&Aring;" />
 
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'''HISTOCOMPATIBILITY ANTIGEN'''<br />
 
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==Overview==
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==HISTOCOMPATIBILITY ANTIGEN==
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To better understand TCR discrimination of multiple ligands, we have, analyzed the crystal structures of two Hb peptide/I-E(k) complexes that, differ by only a single amino acid substitution at the P6 anchor position, within the peptide (E73D). Detailed comparison of multiple independently, determined structures at 1.9 A resolution reveals that removal of a single, buried methylene group can alter a critical portion of the TCR recognition, surface. Significant variance was observed in the peptide P5-P8 main chain, as well as a rotamer difference at LeuP8, approximately 10 A distal from, the substitution. No significant variations were observed in the, conformation of the two MHC class II molecules. The ligand alteration, results in two peptide/MHC complexes that generate bulk T cell responses, that are distinct and essentially nonoverlapping. For the Hb-specific T, cell 3.L2, substitution reduces the potency of the ligand 1000-fold., Soluble 3.L2 TCR binds the two peptide/MHC complexes with similar, affinity, although with faster kinetics. These results highlight the role, of subtle variations in MHC Ag presentation on T cell activation and, signaling.
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<StructureSection load='1fng' size='340' side='right'caption='[[1fng]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fng]] is a 4 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=1FNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FNG 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]] 1.9&#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=1fng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fng OCA], [https://pdbe.org/1fng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fng RCSB], [https://www.ebi.ac.uk/pdbsum/1fng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fng ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HA22_MOUSE HA22_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/fn/1fng_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=1fng ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FNG 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNG OCA].
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*[[MHC 3D structures|MHC 3D structures]]
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*[[MHC II 3D structures|MHC II 3D structures]]
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==Reference==
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__TOC__
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Structural and functional consequences of altering a peptide MHC anchor residue., Kersh GJ, Miley MJ, Nelson CA, Grakoui A, Horvath S, Donermeyer DL, Kappler J, Allen PM, Fremont DH, J Immunol. 2001 Mar 1;166(5):3345-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11207290 11207290]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Fremont DH]]
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[[Category: Fremont, D.H.]]
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[[Category: Miley MJ]]
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[[Category: Miley, M.J.]]
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[[Category: Nelson CA]]
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[[Category: Nelson, C.A.]]
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[[Category: NAG]]
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[[Category: histocompatibility antigen]]
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[[Category: immune system]]
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[[Category: mhc]]
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[[Category: peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:03:55 2007''
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Current revision

HISTOCOMPATIBILITY ANTIGEN

PDB ID 1fng

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