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| [[Image:1d9k.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1d9k| PDB=1d9k | SCENE= }} | | {{STRUCTURE_1d9k| PDB=1d9k | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA'''
| | ===CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10583947}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10583947 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10583947}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mhc class ii]] | | [[Category: Mhc class ii]] |
| [[Category: T-cell receptor]] | | [[Category: T-cell receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:36:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:42:46 2008'' |
