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protein Protein-protein interface(s) links
Complex (immunoglobulin/hydrolase) PDB id
1nsn
Jmol
Contents
Protein chains
217 a.a. *
210 a.a. *
138 a.a. *
* Residue conservation analysis
PDB id:
1nsn
Name: Complex (immunoglobulin/hydrolase)
Title: The crystal structure of antibody n10-staphylococcal nuclease complex at 2.9 angstroms resolution
Structure: 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,
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: caf1. Staphylococcus aureus. Organism_taxid: 1280. Strain: foggi. Gene: nuclease. Expressed in: escherichia coli.
Biol. unit: Trimer (from PQS)
Resolution:
2.80Å     R-factor:   0.195    
Authors: S.Sheriff,P.Bossart-Whitaker
Key ref:
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: 7473734 DOI: 10.1006/jmbi.1995.0573
Date:
06-Jun-95     Release date:   15-Sep-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Protein chain
No UniProt id for this chain
Protein chain
Pfam   ArchSchema ?
P00644  (NUC_STAAU) -  Thermonuclease
Seq:
Struc:
231 a.a.
138 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain S: E.C.3.1.31.1  - Micrococcal nuclease.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleic acid binding     3 terms  

 

 
DOI no: 10.1006/jmbi.1995.0573 J Mol Biol 253:559-575 (1995)
PubMed id: 7473734  
 
 
The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 A resolution.
P.Bossart-Whitaker, C.Y.Chang, J.Novotny, D.C.Benjamin, S.Sheriff.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
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).
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.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1995, 253, 559-575) copyright 1995.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18234071 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.
  BMC Bioinformatics, 9, 71.  
  20526429 C.Yan, V.Honavar, and D.Dobbs (2004).
Identification of interface residues in protease-inhibitor and antigen-antibody complexes: a support vector machine approach.
  Neural Comput Appl, 13, 123-129.  
15146485 M.Geva, M.Eisenstein, and L.Addadi (2004).
Antibody recognition of chiral surfaces. Structural models of antibody complexes with leucine-leucine-tyrosine crystal surfaces.
  Proteins, 55, 862-873.  
11598879 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.
  Biopolymers, 59, 446-456.  
10737939 D.W.Ritchie, and G.J.Kemp (2000).
Protein docking using spherical polar Fourier correlations.
  Proteins, 39, 178-194.  
10771426 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.
  Acta Crystallogr D Biol Crystallogr, 56, 573-580.
PDB code: 1dqd
  11080628 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.
  Structure, 8, 1069-1077.
PDB codes: 1e6j 1e6o
10828942 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(,).
  Biochemistry, 39, 6296-6309.
PDB codes: 1dqj 1dqm 1dqq
10090739 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.
  Biochemistry, 38, 3530-3537.  
  10368281 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.
  Structure, 7, 131-142.
PDB codes: 1f58 2f58 3f58
9692956 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.
  Biochemistry, 37, 10660-10670.  
  9753694 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.
  Structure, 6, 1153-1167.
PDB code: 1bj1
9179436 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.
  Clin Exp Allergy, 27, 593-599.  
8952503 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.
  Biochemistry, 35, 15494-15503.
PDB codes: 1kip 1kiq 1kir
8880929 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.
  Proteins, 26, 55-65.
PDB codes: 1bql 1dkj 1dkk
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.