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PDBsum entry 1cid
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T-cell surface glycoprotein
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PDB id
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1cid
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Contents |
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* Residue conservation analysis
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DOI no:
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Science
260:979-983
(1993)
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PubMed id:
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Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.
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R.L.Brady,
E.J.Dodson,
G.G.Dodson,
G.Lange,
S.J.Davis,
A.F.Williams,
A.N.Barclay.
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ABSTRACT
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The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with
major histocompatibility complex class II antigens and is also a receptor for
the human immunodeficiency virus. the extracellular portion of CD4 is predicted
to fold into four immunoglobulin-like domains. The crystal structure of the
third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and
shows that both domains have immunoglobulin folds. Domain 3, however, lacks the
disulfide between the beta sheets; this results in an expansion of the domain.
There is a difference of 30 degrees in the orientation between domains 3 and 4
when compared with domains 1 and 2. The two CD4 fragment structures provide a
basis from which models of the overall receptor can be proposed. These models
suggest an extended structure comprising two rigid portions joined by a short
and possibly flexible linker region.
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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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Z.D.Zhang,
G.Weinstock,
and
M.Gerstein
(2008).
Rapid evolution by positive Darwinian selection in T-cell antigen CD4 in primates.
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J Mol Evol,
66,
446-456.
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G.W.Lynch,
S.Turville,
B.Carter,
A.J.Sloane,
A.Chan,
N.Muljadi,
S.Li,
L.Low,
P.Armati,
R.Raison,
H.Zoellner,
P.Williamson,
A.Cunningham,
and
W.B.Church
(2006).
Marked differences in the structures and protein associations of lymphocyte and monocyte CD4: resolution of a novel CD4 isoform.
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Immunol Cell Biol,
84,
154-165.
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K.Vermeire,
and
D.Schols
(2005).
Anti-HIV agents targeting the interaction of gp120 with the cellular CD4 receptor.
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Expert Opin Investig Drugs,
14,
1199-1212.
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M.A.Wouters,
K.K.Lau,
and
P.J.Hogg
(2004).
Cross-strand disulphides in cell entry proteins: poised to act.
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Bioessays,
26,
73-79.
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L.J.Matthias,
and
P.J.Hogg
(2003).
Redox control on the cell surface: implications for HIV-1 entry.
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Antioxid Redox Signal,
5,
133-138.
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L.J.Matthias,
P.T.Yam,
X.M.Jiang,
and
P.J.Hogg
(2003).
Disulfide exchange in CD4.
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Biofactors,
17,
241-248.
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P.J.Hogg
(2003).
Disulfide bonds as switches for protein function.
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Trends Biochem Sci,
28,
210-214.
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J.G.Head,
A.Houmeida,
P.J.Knight,
A.R.Clarke,
J.Trinick,
and
R.L.Brady
(2001).
Stability and folding rates of domains spanning the large A-band super-repeat of titin.
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Biophys J,
81,
1570-1579.
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J.H.Wang,
R.Meijers,
Y.Xiong,
J.H.Liu,
T.Sakihama,
R.Zhang,
A.Joachimiak,
and
E.L.Reinherz
(2001).
Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule.
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Proc Natl Acad Sci U S A,
98,
10799-10804.
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PDB code:
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P.Taylor,
M.Bilsland,
and
M.D.Walkinshaw
(2001).
A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement.
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Acta Crystallogr D Biol Crystallogr,
57,
1579-1583.
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PDB code:
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N.Kannan,
T.D.Schneider,
and
S.Vishveshwara
(2000).
Logos for amino-acid preferences in different backbone packing density regions of protein structural classes.
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Acta Crystallogr D Biol Crystallogr,
56,
1156-1165.
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B.Bouma,
P.G.de Groot,
J.M.van den Elsen,
R.B.Ravelli,
A.Schouten,
M.J.Simmelink,
R.H.Derksen,
J.Kroon,
and
P.Gros
(1999).
Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure.
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EMBO J,
18,
5166-5174.
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PDB code:
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G.W.Lynch,
A.J.Sloane,
V.Raso,
A.Lai,
and
A.L.Cunningham
(1999).
Direct evidence for native CD4 oligomers in lymphoid and monocytoid cells.
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Eur J Immunol,
29,
2590-2602.
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B.Arden
(1998).
Conserved motifs in T-cell receptor CDR1 and CDR2: implications for ligand and CD8 co-receptor binding.
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Curr Opin Immunol,
10,
74-81.
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J.Wang,
and
T.A.Springer
(1998).
Structural specializations of immunoglobulin superfamily members for adhesion to integrins and viruses.
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Immunol Rev,
163,
197-215.
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R.Zamoyska
(1998).
CD4 and CD8: modulators of T-cell receptor recognition of antigen and of immune responses?
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Curr Opin Immunol,
10,
82-87.
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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.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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J.H.Simon,
P.Stumbles,
N.Signoret,
C.Somoza,
M.Puklavec,
Q.J.Sattentau,
A.N.Barclay,
and
W.James
(1997).
Role of CD4 epitopes outside the gp120-binding site during entry of human immunodeficiency virus type 1.
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J Virol,
71,
1476-1484.
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A.Bateman,
M.Jouet,
J.MacFarlane,
J.S.Du,
S.Kenwrick,
and
C.Chothia
(1996).
Outline structure of the human L1 cell adhesion molecule and the sites where mutations cause neurological disorders.
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EMBO J,
15,
6050-6059.
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B.Drescher,
E.Spiess,
M.Schachner,
and
R.Probstmeier
(1996).
Structural analysis of the murine cell adhesion molecule L1 by electron microscopy and computer-assisted modelling.
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Eur J Neurosci,
8,
2467-2478.
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D.Willbold,
and
P.Rösch
(1996).
Solution Structure of the Human CD4 (403-419) Receptor Peptide.
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J Biomed Sci,
3,
435-441.
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PDB code:
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H.Wu,
D.G.Myszka,
S.W.Tendian,
C.G.Brouillette,
R.W.Sweet,
I.M.Chaiken,
and
W.A.Hendrickson
(1996).
Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding.
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Proc Natl Acad Sci U S A,
93,
15030-15035.
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PDB codes:
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M.Raghavan,
and
P.J.Bjorkman
(1996).
Fc receptors and their interactions with immunoglobulins.
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Annu Rev Cell Dev Biol,
12,
181-220.
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P.Bork,
A.K.Downing,
B.Kieffer,
and
I.D.Campbell
(1996).
Structure and distribution of modules in extracellular proteins.
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Q Rev Biophys,
29,
119-167.
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S.Improta,
A.S.Politou,
and
A.Pastore
(1996).
Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.
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Structure,
4,
323-337.
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PDB codes:
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S.Moir,
J.Perreault,
and
L.Poulin
(1996).
Postbinding events mediated by human immunodeficiency virus type 1 are sensitive to modifications in the D4-transmembrane linker region of CD4.
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J Virol,
70,
8019-8028.
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W.A.Hendrickson
(1996).
Production of crystallizable fragments of membrane proteins.
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J Bioenerg Biomembr,
28,
35-40.
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J.H.Wang,
R.B.Pepinsky,
T.Stehle,
J.H.Liu,
M.Karpusas,
B.Browning,
and
L.Osborn
(1995).
The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction.
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Proc Natl Acad Sci U S A,
92,
5714-5718.
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PDB code:
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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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R.E.Bachelder,
J.Bilancieri,
W.Lin,
and
N.L.Letvin
(1995).
A human recombinant Fab identifies a human immunodeficiency virus type 1-induced conformational change in cell surface-expressed CD4.
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J Virol,
69,
5734-5742.
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T.Sakihama,
A.Smolyar,
and
E.L.Reinherz
(1995).
Oligomerization of CD4 is required for stable binding to class II major histocompatibility complex proteins but not for interaction with human immunodeficiency virus gp120.
|
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Proc Natl Acad Sci U S A,
92,
6444-6448.
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U.Nörenberg,
M.Hubert,
T.Brümmendorf,
A.Tárnok,
and
F.G.Rathjen
(1995).
Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R.
|
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J Cell Biol,
130,
473-484.
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A.H.Huber,
Y.M.Wang,
A.J.Bieber,
and
P.J.Bjorkman
(1994).
Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A.
|
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Neuron,
12,
717-731.
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PDB code:
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D.A.Vignali,
and
J.L.Strominger
(1994).
Amino acid residues that flank core peptide epitopes and the extracellular domains of CD4 modulate differential signaling through the T cell receptor.
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J Exp Med,
179,
1945-1956.
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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.Gammon,
G.Chandler,
P.Depledge,
C.Elcock,
S.Wrigley,
J.Moore,
G.Cammarota,
F.Sinigaglia,
and
M.Moore
(1994).
A fungal metabolite which inhibits the interaction of CD4 with major histocompatibility complex-encoded class II molecules.
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Eur J Immunol,
24,
991-998.
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G.Lange,
S.J.Lewis,
G.N.Murshudov,
G.G.Dodson,
P.C.Moody,
J.P.Turkenburg,
A.N.Barclay,
and
R.L.Brady
(1994).
Crystal structure of an extracellular fragment of the rat CD4 receptor containing domains 3 and 4.
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Structure,
2,
469-481.
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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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I.D.Campbell,
and
A.K.Downing
(1994).
Building protein structure and function from modular units.
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Trends Biotechnol,
12,
168-172.
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I.D.Campbell,
and
C.Spitzfaden
(1994).
Building proteins with fibronectin type III modules.
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Structure,
2,
333-337.
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L.M.Ptaszek,
S.Vijayakumar,
G.Ravishanker,
and
D.L.Beveridge
(1994).
Molecular dynamics studies of the human CD4 protein.
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Biopolymers,
34,
1145-1153.
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M.G.Rossmann
(1994).
Viral cell recognition and entry.
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Protein Sci,
3,
1712-1725.
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R.Zamoyska
(1994).
The CD8 coreceptor revisited: one chain good, two chains better.
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Immunity,
1,
243-246.
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S.E.Ryu,
A.Truneh,
R.W.Sweet,
and
W.A.Hendrickson
(1994).
Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices.
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Structure,
2,
59-74.
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PDB codes:
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T.J.Dudgeon,
M.J.Bottomley,
P.C.Driscoll,
M.J.Humphries,
A.P.Mould,
G.I.Wingfield,
and
J.M.Clements
(1994).
Expression and characterisation of a very-late antigen-4 (alpha 4 beta 1) integrin-binding fragment of vascular cell-adhesion molecule-1.
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Eur J Biochem,
226,
517-523.
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N.Signoret,
P.Poignard,
D.Blanc,
and
Q.J.Sattentau
(1993).
Human and simian immunodeficiency viruses: virus-receptor interactions.
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Trends Microbiol,
1,
328-333.
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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
