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Contents |
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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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Structure of a heterophilic adhesion complex between the human cd2 and cd58(lfa-3) counter-receptors
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Structure:
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Human cd2 protein. Chain: a, c. Fragment: n-terminal adhesion domain of cd2. Engineered: yes. Mutation: yes. Human cd58 protein. Chain: b, d. Fragment: n-terminal adhesion domain of cd58. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Monomer (from PDB file)
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Resolution:
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3.20Å
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R-factor:
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0.223
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R-free:
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0.281
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Authors:
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J.-H.Wang,A.Smolyar,K.Tan,J.-H.Liu,M.Kim,Z.J.Sun,G.Wagner, E.L.Reinherz
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Key ref:
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J.H.Wang
et al.
(1999).
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.
Cell,
97,
791-803.
PubMed id:
DOI:
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Date:
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13-Apr-99
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Release date:
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29-Apr-99
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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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Cell
97:791-803
(1999)
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PubMed id:
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Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.
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J.H.Wang,
A.Smolyar,
K.Tan,
J.H.Liu,
M.Kim,
Z.Y.Sun,
G.Wagner,
E.L.Reinherz.
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ABSTRACT
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Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing cells
optimizes immune recognition, facilitating contacts between helper T lymphocytes
and antigen-presenting cells as well as between cytolytic effectors and target
cells. Here, we report the crystal structure of the heterophilic adhesion
complex between the amino-terminal domains of human CD2 and CD58. A strikingly
asymmetric, orthogonal, face-to-face interaction involving the major beta sheets
of the respective immunoglobulin-like domains with poor shape complementarity is
revealed. In the virtual absence of hydrophobic forces, interdigitating charged
amino acid side chains form hydrogen bonds and salt links at the interface
(approximately 1200 A2), imparting a high degree of specificity albeit with low
affinity (K(D) of approximately microM). These features explain CD2-CD58 dynamic
binding, offering insights into interactions of related immunoglobulin
superfamily receptors.
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Selected figure(s)
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Figure 2.
Figure 2. Ribbon Drawing of the hCD2–hCD58 Complex in
StereoCD2 is in blue, and hCD58 is in yellow. The β strands in
both molecules were defined by the program DSSP ([38]) and
labeled in black. The figure was generated using the program
MOLSCRIPT ( [40]).
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Figure 5.
Figure 5. Molecular Surface Representation of the Model of
hCD2–hCD58 Ectodomain InteractionThe model was constructed
based on crystal structures of hCD2–hCD58, hCD2–hCD2, and
homology modeling of the second domain of hCD58. The two views
are representative of the same complex rotated  vert,
similar 120° around the vertical axis. The position of the
N-linked glycans attached to asparagine residues are shown in
dark blue with the first glycan linked to Asn-65 of hCD2 in
pink. The T11[3] mAb–binding site is shown in red. GRASP
surface representations of hCD2 and hCD58 are shown in light
blue and yellow, respectively.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1999,
97,
791-803)
copyright 1999.
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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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PDB codes:
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PDB code:
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Crystal structure and binding properties of the CD2 and CD244 (2B4)-binding protein, CD48.
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PDB code:
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(2001).
Herpes simplex virus glycoprotein D bound to the human receptor HveA.
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Mol Cell,
8,
169-179.
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PDB codes:
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M.L.Dustin,
S.K.Bromley,
M.M.Davis,
and
C.Zhu
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Identification of self through two-dimensional chemistry and synapses.
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Annu Rev Cell Dev Biol,
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S.Radaev,
B.Rostro,
A.G.Brooks,
M.Colonna,
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Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3.
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| |
Immunity,
15,
1039-1049.
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PDB code:
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Y.W.Chen
(2001).
Solution solution: using NMR models for molecular replacement.
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Acta Crystallogr D Biol Crystallogr,
57,
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A.Kitao,
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A space-time structure determination of human CD2 reveals the CD58-binding mode.
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Proc Natl Acad Sci U S A,
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D.A.Ostrov,
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J.C.Schwartz,
S.C.Almo,
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S.G.Nathenson
(2000).
Structure of murine CTLA-4 and its role in modulating T cell responsiveness.
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Science,
290,
816-819.
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PDB code:
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H.A.Chen,
M.Pfuhl,
M.S.McAlister,
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Determination of pK(a) values of carboxyl groups in the N-terminal domain of rat CD2: anomalous pK(a) of a glutamate on the ligand-binding surface.
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Biochemistry,
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Structural basis of cell-cell interactions in the immune system.
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M.C.Deller,
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Cell surface receptors.
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E.Chouin,
H.van der Zandt,
J.M.Bergelson,
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(2000).
Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution.
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| |
Structure,
8,
1147-1155.
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PDB codes:
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M.L.Dustin,
and
A.C.Chan
(2000).
Signaling takes shape in the immune system.
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Cell,
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Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition.
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Semin Immunol,
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S.G.Tangye,
J.H.Phillips,
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The CD2-subset of the Ig superfamily of cell surface molecules: receptor-ligand pairs expressed by NK cells and other immune cells.
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Semin Immunol,
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S.Ikemizu,
R.J.Gilbert,
J.A.Fennelly,
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D.I.Stuart,
and
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(2000).
Structure and dimerization of a soluble form of B7-1.
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| |
Immunity,
12,
51-60.
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PDB code:
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Y.W.Chen,
E.J.Dodson,
and
G.J.Kleywegt
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Does NMR mean "not for molecular replacement"? Using NMR-based search models to solve protein crystal structures.
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Structure,
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R213-R220.
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Z.Hu,
B.Ma,
H.Wolfson,
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Conservation of polar residues as hot spots at protein interfaces.
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Proteins,
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P.A.van der Merwe
(1999).
A subtle role for CD2 in T cell antigen recognition.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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