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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Human b7-1/ctla-4 co-stimulatory complex
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Structure:
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T lymphocyte activation antigen cd80. Chain: a, b. Fragment: extracellular domain, residues 35-242. Synonym: activation b7-1 antigen, ctla-4 counter-receptor b7.1. Engineered: yes. Cytotoxic t-lymphocyte protein 4. Chain: c, d. Fragment: extracellular domain, residues 36-161. Synonym: ctla-4, cytotoxic t-lymphocyte-associated antigen 4.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_taxid: 10029
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Resolution:
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3.00Å
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R-factor:
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0.229
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R-free:
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0.257
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Authors:
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C.C.Stamper,W.S.Somers,L.Mosyak
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Key ref:
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C.C.Stamper
et al.
(2001).
Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
Nature,
410,
608-611.
PubMed id:
DOI:
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Date:
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14-Mar-01
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Release date:
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04-Apr-01
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PROCHECK
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Headers
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References
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DOI no:
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Nature
410:608-611
(2001)
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PubMed id:
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Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
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C.C.Stamper,
Y.Zhang,
J.F.Tobin,
D.V.Erbe,
S.Ikemizu,
S.J.Davis,
M.L.Stahl,
J.Seehra,
W.S.Somers,
L.Mosyak.
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ABSTRACT
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Optimal immune responses require both an antigen-specific and a co-stimulatory
signal. The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the
co-stimulatory signal through CD28 and CTLA-4 on T cells. Signalling through
CD28 augments the T-cell response, whereas CTLA-4 signalling attenuates it.
Numerous animal studies and recent clinical trials indicate that manipulating
these interactions holds considerable promise for immunotherapy. With the
consequences of these signals well established, and details of the downstream
signalling events emerging, understanding the molecular nature of these
extracellular interactions becomes crucial. Here we report the crystal structure
of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution. In contrast
to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1
binding interface exhibits an unusually high degree of shape complementarity.
CTLA-4 forms homodimers through a newly defined interface of highly conserved
residues. In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic
arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
This zipper-like oligomerization provides the structural basis for forming
unusually stable signalling complexes at the T-cell surface, underscoring the
importance of potent inhibitory signalling in human immune responses.
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Selected figure(s)
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Figure 2.
Figure 2: Overview of receptor -ligand interactions. a,
Ribbon diagram showing orthogonal interaction between sCTLA-4
(cyan) and sB7-1 (purple) monomers. Also shown is the molecular
surface representation (white transparent) of the ligand-binding
domain of sB7-1 to emphasize the high geometric match between
the two interacting surfaces. b, Direct receptor -ligand
contacts. The 99MYPPPY104 loop of sCTLA-4 is buried in a shallow
depression of the sB7-1 GFCC' surface. Colour coding is as in a.
Three out of five hydrogen bonds formed across the  -sheets
of the interacting domains are depicted as red dashed lines.
Several other side chains on CTLA-4 and B7-1 (not shown) may
contribute to the binding through appreciable, but not direct,
contacts formed on the periphery of the binding interface.
Figure prepared with BobScript30.
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Figure 3.
Figure 3: Molecular association of sCTLA-4 and sB7-1 in the
crystal lattice. Shown are 'skewed zipper' arrays in which
sCTLA-4/sB7-1 complexes would be evenly spaced along membrane
surfaces with a separation of 105 Å. In the perpendicular
direction, across membranes, ligated receptors would span 140 Å.
Geometrically, sugar chains attached at Asn 173 on B7-1 (bottom)
are close to the cell membrane, implying their potential
involvement in interaction with the membrane, perhaps by
stabilizing the orientation of the B7-1 dimers. APC,
antigen-presenting cell. Figure prepared with RIBBONS29.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2001,
410,
608-611)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Where a reference describes a PDB structure, the PDB
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