2axh: Difference between revisions
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<StructureSection load='2axh' size='340' side='right'caption='[[2axh]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2axh' size='340' side='right'caption='[[2axh]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2axh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2axh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AXH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2axh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axh OCA], [https://pdbe.org/2axh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2axh RCSB], [https://www.ebi.ac.uk/pdbsum/2axh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2axh 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=2axh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axh OCA], [https://pdbe.org/2axh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2axh RCSB], [https://www.ebi.ac.uk/pdbsum/2axh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2axh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRBC1_HUMAN TRBC1_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eisele | [[Category: Eisele L]] | ||
[[Category: Guo | [[Category: Guo Y]] | ||
[[Category: Li | [[Category: Li H]] | ||
[[Category: Li | [[Category: Li Y]] | ||
[[Category: Li | [[Category: Li Z]] | ||
[[Category: Vranken | [[Category: Van Vranken S]] | ||
[[Category: Zhao | [[Category: Zhao Y]] | ||
Latest revision as of 11:00, 23 August 2023
Structural highlights
FunctionPublication Abstract from PubMedThe crystal structures of the Vbeta17+ beta chains of two human T cell receptors (TCRs), originally derived from the synovial fluid (SF4) and tissue (C5-1) of a patient with rheumatoid arthritis (RA), have been determined in native (SF4) and mutant (C5-1(F104-->Y/C187-->S)) forms, respectively. These TCR beta chains form homo-dimers in solution and in crystals. Structural comparison reveals that the main-chain conformations in the CDR regions of the C5-1 and SF4 Vbeta17 closely resemble those of a Vbeta17 JM22 in a bound form; however, the CDR3 region shows different conformations among these three Vbeta17 structures. At the side-chain level, conformational differences were observed at the CDR2 regions between our two ligand-free forms and the bound JM22 form. Other significant differences were observed at the Vbeta regions 8-12, 40-44, and 82-88 between C5-1/SF4 and JM22 Vbeta17, implying that there is considerable variability in the structures of very similar beta chains. Structural alignments also reveal a considerable variation in the Vbeta-Cbeta associations, and this may affect ligand recognition. The crystal structures also provide insights into the structure basis of T cell recognition of Mycoplasma arthritidis mitogen (MAM), a superantigen that may be implicated in the development of human RA. Structural comparisons of the Vbeta domains of known TCR structures indicate that there are significant similarities among Vbeta regions that are MAM-reactive, whereas there appear to be significant structural differences among those Vbeta regions that lack MAM-reactivity. It further reveals that CDR2 and framework region (FR) 3 are likely to account for the binding of TCR to MAM. Crystal structures of T cell receptor (beta) chains related to rheumatoid arthritis.,Li H, Van Vranken S, Zhao Y, Li Z, Guo Y, Eisele L, Li Y Protein Sci. 2005 Dec;14(12):3025-38. Epub 2005 Oct 31. PMID:16260763[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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