This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3c60
From Proteopedia
(Difference between revisions)
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3c60.png|left|200px]] | ||
| - | < | + | ==Crystal structure of mouse MHC class II I-Ab/3K peptide complexed with mouse TCR YAe62== |
| - | + | <StructureSection load='3c60' size='340' side='right'caption='[[3c60]], [[Resolution|resolution]] 3.05Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3c60]] is a 8 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=3C60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C60 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lnu|1lnu]], [[3c5z|3c5z]], [[3c6l|3c6l]]</div></td></tr> | |
| - | - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Aa ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), H2-Ab1, H2-iabeta ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3c60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c60 OCA], [https://pdbe.org/3c60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c60 RCSB], [https://www.ebi.ac.uk/pdbsum/3c60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c60 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == 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/c6/3c60_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3c60 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To test whether highly crossreactive alphabeta T cell receptors (TCRs) produced during limited negative selection best illustrate evolutionarily conserved interactions between TCR and major histocompatibility complex (MHC) molecules, we solved the structures of three TCRs bound to the same MHC II peptide (IAb-3K). The TCRs had similar affinities for IAb-3K but varied from noncrossreactive to extremely crossreactive with other peptides and MHCs. Crossreactivity correlated with a shrinking, increasingly hydrophobic TCR-ligand interface, involving fewer TCR amino acids. A few CDR1 and CDR2 amino acids dominated the most crossreactive TCR interface with MHC, including Vbeta8 48Y and 54E and Valpha4 29Y, arranged to impose the familiar diagonal orientation of TCR on MHC. These interactions contribute to MHC binding by other TCRs using related V regions, but not usually so dominantly. These data show that crossreactive TCRs can spotlight the evolutionarily conserved features of TCR-MHC interactions and that these interactions impose the diagonal docking of TCRs on MHC. | ||
| - | + | Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules.,Dai S, Huseby ES, Rubtsova K, Scott-Browne J, Crawford F, Macdonald WA, Marrack P, Kappler JW Immunity. 2008 Mar;28(3):324-34. Epub 2008 Feb 28. PMID:18308592<ref>PMID:18308592</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3c60" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[MHC 3D structures|MHC 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
| - | + | [[Category: Lk3 transgenic mice]] | |
| - | + | [[Category: Dai, S]] | |
| - | == | + | |
| - | + | ||
| - | [[Category: | + | |
| - | [[Category: | + | |
| - | [[Category: Dai, S | + | |
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
[[Category: Immune response]] | [[Category: Immune response]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Mhc ii]] | [[Category: Mhc ii]] | ||
| - | [[Category: Sugar binding protein | + | [[Category: Sugar binding protein-immune system complex]] |
[[Category: Tcr-pmhc complex]] | [[Category: Tcr-pmhc complex]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:34:48 2008'' | ||
Current revision
Crystal structure of mouse MHC class II I-Ab/3K peptide complexed with mouse TCR YAe62
| |||||||||||

