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New page: left|200px<br /><applet load="1d9k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d9k, resolution 3.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1d9k.gif|left|200px]]<br /><applet load="1d9k" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d9k, resolution 3.2&Aring;" />
'''CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA'''<br />


==Overview==
==CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA==
The crystal structure of a complex involving the D10 T cell receptor, (TCR), 16-residue foreign peptide antigen, and the I-Ak self major, histocompatibility complex (MHC) class II molecule is reported at 3.2, angstrom resolution. The D10 TCR is oriented in an orthogonal mode, relative to its peptide-MHC (pMHC) ligand, necessitated by the, amino-terminal extension of peptide residues projecting from the MHC class, II antigen-binding groove as part of a mini beta sheet. Consequently, the, disposition of D10 complementarity-determining region loops is altered, relative to that of most pMHCI-specific TCRs; the latter TCRs assume a, diagonal orientation, although with substantial variability. Peptide, recognition, which involves P-1 to P8 residues, is dominated by the Valpha, domain, which also binds to the class II MHC beta1 helix. That docking is, limited to one segment of MHC-bound peptide offers an explanation for, epitope recognition and altered peptide ligand effects, suggests a, structural basis for alloreactivity, and illustrates how bacterial, superantigens can span the TCR-pMHCII surface.
<StructureSection load='1d9k' size='340' side='right'caption='[[1d9k]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d9k]] is a 10 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=1D9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9K 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]] 3.2&#8491;</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>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=1d9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9k OCA], [https://pdbe.org/1d9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9k RCSB], [https://www.ebi.ac.uk/pdbsum/1d9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TVA2_MOUSE TVA2_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/d9/1d9k_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=1d9k ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented in an orthogonal mode relative to its peptide-MHC (pMHC) ligand, necessitated by the amino-terminal extension of peptide residues projecting from the MHC class II antigen-binding groove as part of a mini beta sheet. Consequently, the disposition of D10 complementarity-determining region loops is altered relative to that of most pMHCI-specific TCRs; the latter TCRs assume a diagonal orientation, although with substantial variability. Peptide recognition, which involves P-1 to P8 residues, is dominated by the Valpha domain, which also binds to the class II MHC beta1 helix. That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.


==About this Structure==
The crystal structure of a T cell receptor in complex with peptide and MHC class II.,Reinherz EL, Tan K, Tang L, Kern P, Liu J, Xiong Y, Hussey RE, Smolyar A, Hare B, Zhang R, Joachimiak A, Chang HC, Wagner G, Wang J Science. 1999 Dec 3;286(5446):1913-21. PMID:10583947<ref>PMID:10583947</ref>
1D9K 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 NDG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D9K OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of a T cell receptor in complex with peptide and MHC class II., Reinherz EL, Tan K, Tang L, Kern P, Liu J, Xiong Y, Hussey RE, Smolyar A, Hare B, Zhang R, Joachimiak A, Chang HC, Wagner G, Wang J, Science. 1999 Dec 3;286(5446):1913-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10583947 10583947]
</div>
<div class="pdbe-citations 1d9k" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Chang H-C]]
[[Category: Chang, H.C.]]
[[Category: Hare B]]
[[Category: Hare, B.]]
[[Category: Hussey RE]]
[[Category: Hussey, R.E.]]
[[Category: Joachimiak A]]
[[Category: Joachimiak, A.]]
[[Category: Kern P]]
[[Category: Kern, P.]]
[[Category: Liu J-H]]
[[Category: Liu, J.H.]]
[[Category: Reinherz EL]]
[[Category: Reinherz, E.L.]]
[[Category: Smolyar A]]
[[Category: Smolyar, A.]]
[[Category: Tan K]]
[[Category: Tan, K.]]
[[Category: Tang L]]
[[Category: Tang, L.]]
[[Category: Wagner G]]
[[Category: Wagner, G.]]
[[Category: Wang J-H]]
[[Category: Wang, J-H.]]
[[Category: Xiong Y]]
[[Category: Xiong, Y.]]
[[Category: Zhang R]]
[[Category: Zhang, R.]]
[[Category: NDG]]
[[Category: d10]]
[[Category: i-ak]]
[[Category: mhc class ii]]
[[Category: t-cell receptor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:06:08 2007''

Latest revision as of 23:53, 20 November 2024

CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA

1d9k, resolution 3.20Å

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