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217 a.a.
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210 a.a.
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138 a.a.
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* Residue conservation analysis
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PDB id:
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Complex (immunoglobulin/hydrolase)
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Title:
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The crystal structure of antibody n10-staphylococcal nuclease complex at 2.9 angstroms resolution
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Structure:
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Igg fab (igg1, kappa). Chain: l. Synonym: n10 fab immunoglobulin. Igg fab (igg1, kappa). Chain: h. Synonym: n10 fab immunoglobulin. Staphylococcal nuclease. Chain: s. Synonym: staphylococcal nuclease ribonucleate,
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Strain: caf1. Staphylococcus aureus. Organism_taxid: 1280. Strain: foggi. Gene: nuclease. Expressed in: escherichia coli.
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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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S.Sheriff,P.Bossart-Whitaker
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Key ref:
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P.Bossart-Whitaker
et al.
(1995).
The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 A resolution.
J Mol Biol,
253,
559-575.
PubMed id:
DOI:
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Date:
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06-Jun-95
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Release date:
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15-Sep-95
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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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Enzyme class:
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Chain S:
E.C.3.1.31.1
- Micrococcal nuclease.
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Reaction:
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Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
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Gene Ontology (GO) functional annotation
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Biochemical function
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nucleic acid binding
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3 terms
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DOI no:
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J Mol Biol
253:559-575
(1995)
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PubMed id:
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The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 A resolution.
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P.Bossart-Whitaker,
C.Y.Chang,
J.Novotny,
D.C.Benjamin,
S.Sheriff.
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ABSTRACT
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The three-dimensional structure of the antibody N10 Fab fragment complexed with
staphylococcal nuclease (SNase) has been determined to 2.9 A resolution.
Eighteen residues from six complementarity-determining regions (CDR) recognize
an epitope of five distinct SNase segments with a total of 17 residues. The
overall shape of the antibody-antigen interface is U-shaped rather than the more
or less rectangular interface seen in other antibody-protein antigen interfaces.
Despite the U-shaped interface, the amount of surface buried in the complex, 828
A2 for SNase and 793 A2 for N10, is typical of antibody-protein antigen
complexes. Contributing to the shape of the interface is the shortest antibody
heavy chain-CDR3 loop reported to date, which probably allows access of bulk
solvent in the center of the "U" interface. Another unusual feature of
the N10 antibody is the 15 residue antibody light chain-CDR1, a length seen in
only three other reported antibodies. Antibody light chain-CDR1 displays a
previously unobserved conformation in its distal portion. Finally, although some
of the movement observed in the antibody-bound SNase may be due to crystal
contacts, it is clear that some side-chain rearrangements are the result of
antigen-antibody interaction.
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Selected figure(s)
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Figure 1.
Figure 1. Stereo diagram of the N10--SNase complex is shown as a ribbon structure. SNase is shown in cyan with
the epitope contact residues in red. The N10 antibody heavy chain is in green and the light chain in yellow. For both
heavy chain and light chain, the CDR regions are colored silver and the contact residues are in magenta. Figure produced
with RIBBONS (Carson, 1991).
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Figure 7.
Figure 7. Stereo diagram of the chain trace of CDR L1
of Fabs N10 (cyan), 40--50 (red), 50.1 (magenta), 59.1
(yellow). In addition, side-chains of N10 residues Phe
L-30, Tyr L-32 and Trp L-92 are shown in cyan and
canonical base residues (Ile L-2, Ala L-25, Val L-27B, Met
L-33 and Phe L-71) are shown in dark blue. Figure
produced with MOLSCRIPT (Kraulis, 1991) ``turn''
command so that tubes run through C
a
positions.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
253,
559-575)
copyright 1995.
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Figures were
selected
by the author.
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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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V.Moreau,
C.Fleury,
D.Piquer,
C.Nguyen,
N.Novali,
S.Villard,
D.Laune,
C.Granier,
and
F.Molina
(2008).
PEPOP: computational design of immunogenic peptides.
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BMC Bioinformatics, 9,
71.
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C.Yan,
V.Honavar,
and
D.Dobbs
(2004).
Identification of interface residues in protease-inhibitor and antigen-antibody complexes: a support vector machine approach.
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Neural Comput Appl, 13,
123-129.
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M.Geva,
M.Eisenstein,
and
L.Addadi
(2004).
Antibody recognition of chiral surfaces. Structural models of antibody complexes with leucine-leucine-tyrosine crystal surfaces.
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Proteins, 55,
862-873.
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B.Piekarska,
L.Konieczny,
J.Rybarska,
B.Stopa,
G.Zemanek,
E.Szneler,
M.Król,
M.Nowak,
and
I.Roterman
(2001).
Heat-induced formation of a specific binding site for self-assembled Congo Red in the V domain of immunoglobulin L chain lambda.
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Biopolymers, 59,
446-456.
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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.M.Wright,
A.M.Brzozowski,
R.E.Hubbard,
A.C.Pike,
S.M.Roberts,
R.N.Skovgaard,
I.Svendsen,
H.Vissing,
and
R.P.Bywater
(2000).
Structure of Fab hGR-2 F6, a competitive antagonist of the glucagon receptor.
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Acta Crystallogr D Biol Crystallogr, 56,
573-580.
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PDB code:
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S.Monaco-Malbet,
C.Berthet-Colominas,
A.Novelli,
N.Battaï,
N.Piga,
V.Cheynet,
F.Mallet,
and
S.Cusack
(2000).
Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24.
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Structure, 8,
1069-1077.
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PDB codes:
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Y.Li,
H.Li,
S.J.Smith-Gill,
and
R.A.Mariuzza
(2000).
Three-dimensional structures of the free and antigen-bound Fab from monoclonal antilysozyme antibody HyHEL-63(,).
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Biochemistry, 39,
6296-6309.
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PDB codes:
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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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R.Stanfield,
E.Cabezas,
A.Satterthwait,
E.Stura,
A.Profy,
and
I.Wilson
(1999).
Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs.
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Structure, 7,
131-142.
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PDB codes:
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P.S.Pruett,
and
G.M.Air
(1998).
Critical interactions in binding antibody NC41 to influenza N9 neuraminidase: amino acid contacts on the antibody heavy chain.
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Biochemistry, 37,
10660-10670.
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Y.A.Muller,
Y.Chen,
H.W.Christinger,
B.Li,
B.C.Cunningham,
H.B.Lowman,
and
A.M.de Vos
(1998).
VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface.
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Structure, 6,
1153-1167.
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PDB code:
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A.M.Smith,
and
M.D.Chapman
(1997).
Localization of antigenic sites on Der p 2 using oligonucleotide-directed mutagenesis targeted to predicted surface residues.
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Clin Exp Allergy, 27,
593-599.
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B.A.Fields,
F.A.Goldbaum,
W.Dall'Acqua,
E.L.Malchiodi,
A.Cauerhff,
F.P.Schwarz,
X.Ysern,
R.J.Poljak,
and
R.A.Mariuzza
(1996).
Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.
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Biochemistry, 35,
15494-15503.
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PDB codes:
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S.Chacko,
E.W.Silverton,
S.J.Smith-Gill,
D.R.Davies,
K.A.Shick,
K.A.Xavier,
R.C.Willson,
P.D.Jeffrey,
C.Y.Chang,
L.C.Sieker,
and
S.Sheriff
(1996).
Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment.
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Proteins, 26,
55-65.
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PDB codes:
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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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