Publikationsdatum:
1999-12-03
Beschreibung:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinherz, E L -- Tan, K -- Tang, L -- Kern, P -- Liu, J -- Xiong, Y -- Hussey, R E -- Smolyar, A -- Hare, B -- Zhang, R -- Joachimiak, A -- Chang, H C -- Wagner, G -- Wang, J -- AI/CA37581/AI/NIAID NIH HHS/ -- AI19807/AI/NIAID NIH HHS/ -- GM56008/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1913-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunobiology, Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10583947" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Animals
;
Antigens/*chemistry/immunology/metabolism
;
Binding Sites
;
CD4-Positive T-Lymphocytes/immunology
;
CD8-Positive T-Lymphocytes/immunology
;
Conalbumin/chemistry/immunology
;
Crystallization
;
Crystallography, X-Ray
;
Histocompatibility Antigens Class I/immunology
;
Histocompatibility Antigens Class II/*chemistry/immunology/metabolism
;
Hydrogen Bonding
;
Ligands
;
Mice
;
Mice, Inbred AKR
;
Models, Molecular
;
Oligopeptides/chemistry/immunology/metabolism
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Receptors, Antigen, T-Cell, alpha-beta/*chemistry/immunology/metabolism
;
Superantigens/immunology/metabolism
;
Thymus Gland/cytology/immunology
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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