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PDBsum entry 2z35
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Immune system
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PDB id
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2z35
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References listed in PDB file
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Key reference
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Title
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Structural evidence for a germline-Encoded t cell receptor-Major histocompatibility complex interaction 'Codon'.
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Authors
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D.Feng,
C.J.Bond,
L.K.Ely,
J.Maynard,
K.C.Garcia.
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Ref.
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Nat Immunol, 2007,
8,
975-983.
[DOI no: ]
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PubMed id
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Abstract
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All complexes of T cell receptors (TCRs) bound to peptide-major
histocompatibility complex (pMHC) molecules assume a stereotyped binding
'polarity', despite wide variations in TCR-pMHC docking angles. However,
existing TCR-pMHC crystal structures have failed to show broadly conserved
pairwise interaction motifs. Here we determined the crystal structures of two
TCRs encoded by the variable beta-chain 8.2 (V(beta)8.2), each bound to the MHC
class II molecule I-A(u), and did energetic mapping of V(alpha) and V(beta)
contacts with I-A(u). Together with two previously solved structures of
V(beta)8.2-containing TCR-MHC complexes, we found four TCR-I-A complexes with
structurally superimposable interactions between the V(beta) loops and the I-A
alpha-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire
demonstrates what is probably one of many germline-derived TCR-MHC interaction
'codons'.
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Figure 3.
(a) Structures of 1934.4, cl19 and 172.10 from TCR-pMHC
complexes superimposed on I-A^u (colors as in Fig. 1). Red
dashed lines, hydrogen bonds. (b) Interactions between TCR CDR1
 and
CDR2 loops
and the I-A  -helix.
Highlighting indicates residues involved in interactions; black
dashed lines, van der Waals forces; red dashed lines, hydrogen
bonds. Top, interactions of 1934.4.
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Figure 5.
Yellow, peptide; red dashed lines, hydrogen bonds; black
dashed lines, van der Waals interactions. TCR amino acids are
designated by one-letter amino acid code followed by position
number; peptide amino acids are designated by position (P)
number, followed by the one-letter amino acid code. Below,
two-dimensional projections of the CDR3-peptide contacts. (a)
The 1934.4 complex. (b) The cl19 complex. (c) The 172.10 complex.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Immunol
(2007,
8,
975-983)
copyright 2007.
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