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216 a.a.
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210 a.a.
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12 a.a.
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* Residue conservation analysis
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PDB id:
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Immunoglobulin
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Title:
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Crystal structure of an anticholera toxin peptide complex at 2.3 angstroms
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Structure:
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Igg1 te33 fab (light chain). Chain: l. Igg1 te33 fab (heavy chain). Chain: h. Cholera toxin peptide 3 (ctp3). Chain: p. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090.
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Biol. unit:
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Trimer (from
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Resolution:
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Authors:
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M.Shoham
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Key ref:
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M.Shoham
(1993).
Crystal structure of an anticholera toxin peptide complex at 2.3 A.
J Mol Biol,
232,
1169-1175.
PubMed id:
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Date:
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21-Jun-93
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Release date:
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31-Jan-94
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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J Mol Biol
232:1169-1175
(1993)
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PubMed id:
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Crystal structure of an anticholera toxin peptide complex at 2.3 A.
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M.Shoham.
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ABSTRACT
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Cholera toxin peptide 3 (CTP3) is a 15-residue peptide corresponding in sequence
to an immunogenic loop on the surface of the B-subunits of both cholera toxin
and the heat-labile toxin from Escherichia coli. TE33 is the Fab fragment of a
monoclonal antibody elicited against CTP3. The crystal structure of the
TE33-CTP3 complex at 2.3 A resolution reveals an antigen-binding pocket, 13 A
deep and 13 A wide, which is lined with many aromatic residues. The N-terminal
portion of the peptide antigen CTP3 forms a type II beta-turn that fits snugly
into this pocket. At gln7 the peptide backbone of CTP3 forms a kink followed by
an extended C-terminal chain that seals off the cleft and buries the beta-turn
underneath it. All six complementarity-determining regions of TE33 contribute to
the binding of CTP3. The antibody-peptide contacts include, in addition to van
der Waals' interactions and hydrogen bonds, also one salt bridge and one water
molecule, which mediates the interaction.
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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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P.Scheerer,
A.Kramer,
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H.Wessner,
C.Scholz,
N.Krauss,
J.Schneider-Mergener,
and
W.Höhne
(2007).
Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition.
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J Mol Recognit,
20,
263-274.
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PDB code:
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L.Otte,
T.Knaute,
J.Schneider-Mergener,
and
A.Kramer
(2006).
Molecular basis for the binding polyspecificity of an anti-cholera toxin peptide 3 monoclonal antibody.
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J Mol Recognit,
19,
49-59.
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M.J.Clément,
A.Fortuné,
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(2006).
Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a.
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J Biol Chem,
281,
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P.J.Cachia,
D.J.Kao,
and
R.S.Hodges
(2004).
Synthetic peptide vaccine development: measurement of polyclonal antibody affinity and cross-reactivity using a new peptide capture and release system for surface plasmon resonance spectroscopy.
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J Mol Recognit,
17,
540-557.
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S.C.Song,
M.Czerwinski,
B.S.Wojczyk,
and
S.L.Spitalnik
(2004).
Alteration of amino acid residues at the L-chain N-terminus and in complementarity-determining region 3 increases affinity of a recombinant F(ab) for the human N blood group antigen.
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Transfusion,
44,
173-186.
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G.B.Chavali,
A.C.Papageorgiou,
K.A.Olson,
J.W.Fett,
G.Hu,
R.Shapiro,
and
K.R.Acharya
(2003).
The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody.
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Structure,
11,
875-885.
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PDB code:
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P.J.Cachia,
and
R.S.Hodges
(2003).
Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa.
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Biopolymers,
71,
141-168.
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D.J.Tantillo,
and
K.N.Houk
(2001).
Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state.
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Chem Biol,
8,
535-545.
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P.V.Afonin,
A.V.Fokin,
I.N.Tsygannik,
I.Y.Mikhailova,
L.V.Onoprienko,
I.I.Mikhaleva,
V.T.Ivanov,
T.Y.Mareeva,
V.A.Nesmeyanov,
N.Li,
W.A.Pangborn,
W.L.Duax,
and
V.Z.Pletnev
(2001).
Crystal structure of an anti-interleukin-2 monoclonal antibody Fab complexed with an antigenic nonapeptide.
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Protein Sci,
10,
1514-1521.
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PDB code:
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A.P.Campbell,
W.Y.Wong,
R.T.Irvin,
and
B.D.Sykes
(2000).
Interaction of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK with a cross-reactive antibody: conformation of the bound peptide.
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Biochemistry,
39,
14847-14864.
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D.W.Ritchie,
and
G.J.Kemp
(2000).
Protein docking using spherical polar Fourier correlations.
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Proteins,
39,
178-194.
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L.Choulier,
V.Lafont,
N.Hugo,
and
D.Altschuh
(2000).
Covariance analysis of protein families: the case of the variable domains of antibodies.
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Proteins,
41,
475-484.
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U.Lamminmäki,
and
J.Kankare
(2000).
Crystallization and preliminary X-ray analysis of a recombinant Fab fragment in complex with 17beta-oestradiol.
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Acta Crystallogr D Biol Crystallogr,
56,
1670-1672.
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J.L.Torán,
L.Kremer,
L.Sánchez-Pulido,
I.M.de Alborán,
G.del Real,
M.Llorente,
A.Valencia,
M.A.de Mon,
and
C.Martínez-A
(1999).
Molecular analysis of HIV-1 gp120 antibody response using isotype IgM and IgG phage display libraries from a long-term non-progressor HIV-1-infected individual.
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Eur J Immunol,
29,
2666-2675.
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L.Choulier,
N.Rauffer-Bruyère,
M.Ben Khalifa,
F.Martin,
T.Vernet,
and
D.Altschuh
(1999).
Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein.
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Biochemistry,
38,
3530-3537.
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M.Ferrer,
B.J.Sullivan,
K.L.Godbout,
E.Burke,
H.S.Stump,
J.Godoy,
A.Golden,
A.T.Profy,
and
M.R.van Schravendijk
(1999).
Structural and functional characterization of an epitope in the conserved C-terminal region of HIV-1 gp120.
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J Pept Res,
54,
32-42.
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R.D.Stigler,
B.Hoffmann,
R.Abagyan,
and
J.Schneider-Mergener
(1999).
Soft docking an L and a D peptide to an anticholera toxin antibody using internal coordinate mechanics.
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Structure,
7,
663-670.
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A.Rodríguez-Romero,
O.Almog,
M.Tordova,
Z.Randhawa,
and
G.L.Gilliland
(1998).
Primary and tertiary structures of the Fab fragment of a monoclonal anti-E-selectin 7A9 antibody that inhibits neutrophil attachment to endothelial cells.
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J Biol Chem,
273,
11770-11775.
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PDB code:
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F.E.Romesberg,
B.Spiller,
P.G.Schultz,
and
R.C.Stevens
(1998).
Immunological origins of binding and catalysis in a Diels-Alderase antibody.
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Science,
279,
1929-1933.
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PDB codes:
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K.Lim,
S.M.Owens,
L.Arnold,
J.C.Sacchettini,
and
D.S.Linthicum
(1998).
Crystal structure of monoclonal 6B5 Fab complexed with phencyclidine.
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J Biol Chem,
273,
28576-28582.
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PDB code:
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P.Rondard,
and
H.Bedouelle
(1998).
A mutational approach shows similar mechanisms of recognition for the isolated and integrated versions of a protein epitope.
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J Biol Chem,
273,
34753-34759.
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S.Vasudevan,
T.Tsuruo,
and
D.R.Rose
(1998).
Mode of binding of anti-P-glycoprotein antibody MRK-16 to its antigen. A crystallographic and molecular modeling study.
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J Biol Chem,
273,
25413-25419.
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PDB code:
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A.P.Campbell,
D.L.Bautista,
B.Tripet,
W.Y.Wong,
R.T.Irvin,
R.S.Hodges,
and
B.D.Sykes
(1997).
Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.
|
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Biochemistry,
36,
12791-12801.
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J.A.Hubbard,
D.P.Raleigh,
J.R.Bonnerjea,
and
C.M.Dobson
(1997).
Identification of the epitopes of calcitonin gene-related peptide (CGRP) for two anti-CGRP monoclonal antibodies by 2D NMR.
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Protein Sci,
6,
1945-1952.
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T.Keitel,
A.Kramer,
H.Wessner,
C.Scholz,
J.Schneider-Mergener,
and
W.Höhne
(1997).
Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity.
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Cell,
91,
811-820.
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PDB codes:
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P.Orlewski,
M.Marraud,
M.T.Cung,
V.Tsikaris,
M.Sakarellos-Daitsiotis,
C.Sakarellos,
E.Vatzaki,
and
S.J.Tzartos
(1996).
Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data.
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Biopolymers,
40,
419-432.
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PDB codes:
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A.R.Neurath,
N.Strick,
and
A.K.Debnath
(1995).
Structural requirements for and consequences of an antiviral porphyrin binding to the V3 loop of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp120.
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J Mol Recognit,
8,
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G.Siligardi,
and
A.F.Drake
(1995).
The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides.
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Biopolymers,
37,
281-292.
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J.Anglister,
T.Scherf,
B.Zilber,
and
R.Levy
(1995).
Two-dimensional NMR studies of the interactions between a peptide of cholera toxin and monoclonal antibodies.
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Biopolymers,
37,
383-389.
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R.L.Stanfield,
and
I.A.Wilson
(1995).
Protein-peptide interactions.
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Curr Opin Struct Biol,
5,
103-113.
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I.A.Wilson,
and
R.L.Stanfield
(1994).
Antibody-antigen interactions: new structures and new conformational changes.
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Curr Opin Struct Biol,
4,
857-867.
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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
