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PDBsum entry 1fyt
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Immune system
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PDB id
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1fyt
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Contents |
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180 a.a.
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179 a.a.
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13 a.a.
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198 a.a.
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240 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of a covalently stabilized complex of a human alphabeta t-Cell receptor, Influenza ha peptide and mhc class ii molecule, Hla-Dr1.
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Authors
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J.Hennecke,
A.Carfi,
D.C.Wiley.
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Ref.
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Embo J, 2000,
19,
5611-5624.
[DOI no: ]
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PubMed id
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Abstract
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An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA) peptide/human
leukocyte antigen (HLA)-DR1 complex was stabilized by flexibly linking the HA
peptide with the human HA1.7 alphabetaTCR, to increase the local concentration
of the interacting proteins once the peptide has been loaded onto the major
histocompatibility complex (MHC) molecule. The structure of the complex,
determined by X-ray crystallography, has a binding mode similar to that of the
human B7 alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues
contacted are at the same positions observed earlier in class I MHC/peptide/TCR
complexes. One contact, to an MHC loop outside the peptide-binding site, is
conserved and specific to pMHCII complexes. TCR gene usage in the response to
HA/HLA-DR appears to conserve charged interactions between three lysines of the
peptide and acidic residues on the TCR.
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Figure 3.
Figure 3 Interaction of TCR HA1.7 with HLA-DR1 and HA peptide.
(A) TCR contacts. Contacts of CDR residues (solid red lines)
with HLA-DR1 (solid blue lines) and the HA peptide (solid black
line) are indicated by dashed green and dashed red lines,
respectively. Human MHC class II conserved (filled circles) and
polymorphic residues (open circles) are shown. (B) Contacts
between CDR2  and
the conserved Lys39 of DR1  outside
of the peptide-binding site (van der Waals contacts, dashed
black lines; potential hydrogen bonds, dashed red lines). (C)
MHC–peptide solvent-accessible surface buried by the TCR,
colored by CDR type (see key). The total accessible surfaces
buried on pMHC by the TCR are 1111 Å^2 for HA1.7/DR1/HA,
1041 Å^2 for D10/I-Ak/CA, 1031 Å^2 for A6/A2/TAX,
918 Å^2 for B7/A2/TAX and 1111 Å^2 for
2C/H-2Kb/DEV8. The antigenic peptide is shown by a white line.
Figures were prepared with MOLSCRIPT (Kraulis, 1991), Raster3D
(Merritt and Murphy, 1994) and GRASP (Nicholls et al., 1991).
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Figure 4.
Figure 4 Recognition of the HA peptide by TCR HA1.7. (A) Binding
of the HA peptide (yellow) to the surface of the TCR HA1.7 (top)
and in the groove of DR1 (bottom). HA1.7 and DR1 were moved
apart and rotated around the long axis of the peptide by
-20° and +20°, respectively, in order to allow a better
view into the peptide-binding sites. Positive and negative
electrostatic surface potentials of HA1.7 and DR1 are indicated
in blue and red, respectively. (B) van der Waals contacts and
potential hydrogen bonds between TCR HA1.7 and HA peptide are
shown by black and red dashed lines, respectively. (C)
Electrostatic interactions between the three lysines (P–1, P3
and P8) of HA with acidic residues of HA1.7 TCR. (D) HA and CA
peptide residues that are contacted by TCR HA1.7 and D10,
respectively, are shown in red. The number of peptide residues
that are contacted by the different TCRs and the range over
which they are distributed are indicated. (A–C) were prepared
with MOLSCRIPT (Kraulis, 1991), Raster3D (Merritt and Murphy,
1994) and GRASP (Nicholls et al., 1991).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Embo J
(2000,
19,
5611-5624)
copyright 2000.
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