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PDBsum entry 1cdb
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T lymphocyte adhesion glycoprotein
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PDB id
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1cdb
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Contents |
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* Residue conservation analysis
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Structure
1:69-81
(1993)
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PubMed id:
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Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2.
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J.M.Withka,
D.F.Wyss,
G.Wagner,
A.R.Arulanandam,
E.L.Reinherz,
M.A.Recny.
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ABSTRACT
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BACKGROUND: CD2, a T-cell specific surface glycoprotein, is critically important
for mediating adherence of T cells to antigen-presenting cells or target cells.
Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3)
expressed on the cell to which the T cell binds. Human CD2 domain 1 requires
N-linked carbohydrate to maintain its native conformation and ability to bind
CD58. In contrast, rat CD2 does not require N-linked carbohydrate, and binds to
a different ligand, CD48. RESULTS: The three-dimensional structure of the
glycosylated form of domain 1 of human CD2 has been determined by NMR
spectroscopy. The overall structure resembles the typical beta-barrel of an
immunoglobulin variable domain. Nuclear Overhauser enhancement contacts between
the protein and the N-linked glycan have been tentatively identified.
CONCLUSION: Based on our results, we propose a model showing how the N-linked
glycan might be positioned in the human CD2 domain 1 structure. The model
provides an explanation for the observed instability of deglycosylated human
CD2, and allows residues that are important for CD58 binding to be
differentiated from those affecting conformational stability via interactions
with the glycan.
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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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Y.Liu,
Q.Tong,
Y.Zhou,
H.W.Lee,
J.J.Yang,
H.J.Bühring,
Y.T.Chen,
B.Ha,
C.X.Chen,
Y.Yang,
and
K.Zen
(2007).
Functional elements on SIRPalpha IgV domain mediate cell surface binding to CD47.
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J Mol Biol,
365,
680-693.
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A.Kitao,
and
G.Wagner
(2006).
Amplitudes and directions of internal protein motions from a JAM analysis of 15N relaxation data.
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Magn Reson Chem,
44,
S130-S142.
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J.Liu,
J.Ying,
V.T.Chow,
V.J.Hruby,
and
S.D.Satyanarayanajois
(2005).
Structure-activity studies of peptides from the "hot-spot" region of human CD2 protein: development of peptides for immunomodulation.
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J Med Chem,
48,
6236-6249.
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L.Jining,
I.Makagiansar,
H.Yusuf-Makagiansar,
V.T.Chow,
T.J.Siahaan,
and
S.D.Jois
(2004).
Design, structure and biological activity of beta-turn peptides of CD2 protein for inhibition of T-cell adhesion.
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Eur J Biochem,
271,
2873-2886.
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M.Shimojima,
Y.Nishimura,
T.Miyazawa,
K.Kato,
K.Nakamura,
Y.Izumiya,
H.Akashi,
and
Y.Tohya
(2002).
A feline CD2 homologue interacts with human red blood cells.
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Immunology,
105,
360-366.
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D.Bailey,
D.V.Renouf,
D.G.Large,
C.D.Warren,
and
E.F.Hounsell
(2000).
Conformational studies of the glycopeptide Ac-Tyr-[Man5GlcNAc-beta-(1-->4)GlcNAc-beta-(1-->Ndelta)]-Asn-Leu-Thr-Se r-OBz and the constituent peptide and oligosaccharide.
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Carbohydr Res,
324,
242-254.
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H.A.Chen,
M.Pfuhl,
M.S.McAlister,
and
P.C.Driscoll
(2000).
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,
39,
6814-6824.
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J.H.Wang,
A.Smolyar,
K.Tan,
J.H.Liu,
M.Kim,
Z.Y.Sun,
G.Wagner,
and
E.L.Reinherz
(1999).
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.
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Cell,
97,
791-803.
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PDB code:
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Z.Y.Sun,
V.Dötsch,
M.Kim,
J.Li,
E.L.Reinherz,
and
G.Wagner
(1999).
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.
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EMBO J,
18,
2941-2949.
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PDB code:
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J.Li,
K.Nishizawa,
W.An,
R.E.Hussey,
F.E.Lialios,
R.Salgia,
R.Sunder-Plassmann,
and
E.L.Reinherz
(1998).
A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.
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EMBO J,
17,
7320-7336.
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S.J.Davis,
S.Ikemizu,
M.K.Wild,
and
P.A.van der Merwe
(1998).
CD2 and the nature of protein interactions mediating cell-cell recognition.
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Immunol Rev,
163,
217-236.
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C.Chothia,
and
E.Y.Jones
(1997).
The molecular structure of cell adhesion molecules.
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Annu Rev Biochem,
66,
823-862.
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D.F.Wyss,
K.T.Dayie,
and
G.Wagner
(1997).
The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions.
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Protein Sci,
6,
534-542.
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D.J.Leahy
(1997).
Implications of atomic-resolution structures for cell adhesion.
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Annu Rev Cell Dev Biol,
13,
363-393.
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A.M.Krezel,
C.Kasibhatla,
P.Hidalgo,
R.MacKinnon,
and
G.Wagner
(1995).
Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry.
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Protein Sci,
4,
1478-1489.
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PDB code:
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C.L.Holness,
P.A.Bates,
A.J.Little,
C.D.Buckley,
A.McDowall,
D.Bossy,
N.Hogg,
and
D.L.Simmons
(1995).
Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1.
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J Biol Chem,
270,
877-884.
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J.G.Wall,
and
A.Plückthun
(1995).
Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli.
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Curr Opin Biotechnol,
6,
507-516.
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P.A.van der Merwe,
P.N.McNamee,
E.A.Davies,
A.N.Barclay,
and
S.J.Davis
(1995).
Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells.
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Curr Biol,
5,
74-84.
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S.J.Davis,
E.A.Davies,
A.N.Barclay,
S.Daenke,
D.L.Bodian,
E.Y.Jones,
D.I.Stuart,
T.D.Butters,
R.A.Dwek,
and
P.A.van der Merwe
(1995).
Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent.
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J Biol Chem,
270,
369-375.
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A.Helenius
(1994).
How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.
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Mol Biol Cell,
5,
253-265.
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A.R.Arulanandam,
A.Kister,
M.J.McGregor,
D.F.Wyss,
G.Wagner,
and
E.L.Reinherz
(1994).
Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains.
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J Exp Med,
180,
1861-1871.
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D.L.Bodian,
E.Y.Jones,
K.Harlos,
D.I.Stuart,
and
S.J.Davis
(1994).
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
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Structure,
2,
755-766.
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PDB code:
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G.Wagner,
and
D.F.Wyss
(1994).
Cell surface adhesion receptors.
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Curr Opin Struct Biol,
4,
841-851.
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A.R.Arulanandam,
J.M.Withka,
D.F.Wyss,
G.Wagner,
A.Kister,
P.Pallai,
M.A.Recny,
and
E.L.Reinherz
(1993).
The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain.
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Proc Natl Acad Sci U S A,
90,
11613-11617.
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C.M.Fletcher,
R.A.Harrison,
P.J.Lachmann,
and
D.Neuhaus
(1993).
Sequence-specific 1H-NMR assignments and folding topology of human CD59.
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Protein Sci,
2,
2015-2027.
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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
code is
shown on the right.
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Links
