1d9k
From Proteopedia
(New page: 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=" | + | [[Image:1d9k.gif|left|200px]]<br /><applet load="1d9k" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d9k, resolution 3.2Å" /> | caption="1d9k, resolution 3.2Å" /> | ||
'''CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA'''<br /> | '''CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a complex involving the D10 T cell receptor | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Chang, H | + | [[Category: Chang, H C.]] |
[[Category: Hare, B.]] | [[Category: Hare, B.]] | ||
| - | [[Category: Hussey, R | + | [[Category: Hussey, R E.]] |
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
[[Category: Kern, P.]] | [[Category: Kern, P.]] | ||
| - | [[Category: Liu, J | + | [[Category: Liu, J H.]] |
| - | [[Category: Reinherz, E | + | [[Category: Reinherz, E L.]] |
[[Category: Smolyar, A.]] | [[Category: Smolyar, A.]] | ||
[[Category: Tan, K.]] | [[Category: Tan, K.]] | ||
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[[Category: t-cell receptor]] | [[Category: t-cell receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:21 2008'' |
Revision as of 10:14, 21 February 2008
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CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA
Overview
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
1D9K is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:14:21 2008
Categories: Mus musculus | Protein complex | Chang, H C. | Hare, B. | Hussey, R E. | Joachimiak, A. | Kern, P. | Liu, J H. | Reinherz, E L. | Smolyar, A. | Tan, K. | Tang, L. | Wagner, G. | Wang, J-H. | Xiong, Y. | Zhang, R. | NDG | D10 | I-ak | Mhc class ii | T-cell receptor
