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PDBsum entry 1fvb
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protein Protein-protein interface(s) links
Immunoglobulin PDB id
1fvb

 

 

 

 

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Contents
Protein chains
106 a.a.
119 a.a.
Theoretical model
PDB id:
1fvb
Name: Immunoglobulin
Structure: Ig A fv fragment (19.1.2, anti-alpha(1(right arrow)6) dextran) (theoretical model)
Source: Mouse (mus musculus)
Authors: E.A.Padlan,E.A.Kabat
Key ref: E.A.Padlan and E.A.Kabat (1988). Model-building study of the combining sites of two antibodies to alpha (1----6)dextran. Proc Natl Acad Sci U S A, 85, 6885-6889. PubMed id: 2457920 DOI: 10.1073/pnas.85.18.6885
Date:
09-Apr-88     Release date:   19-Apr-89    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 106 a.a.
Protein chain
No UniProt id for this chain
Struc: 119 a.a.
Key:    Secondary structure

 

 
DOI no: 10.1073/pnas.85.18.6885 Proc Natl Acad Sci U S A 85:6885-6889 (1988)
PubMed id: 2457920  
 
 
Model-building study of the combining sites of two antibodies to alpha (1----6)dextran.
E.A.Padlan, E.A.Kabat.
 
  ABSTRACT  
 
Models of the Fv portion (containing the variable regions of the heavy and light chains) of two monoclonal anti-alpha (1----6)dextran antibodies, W3129 and 19.1.2, were constructed from amino acid sequences and the known three-dimensional structures of the Fv portions of McPC603 and J539. The modeled combining site of W3129 has a protrusion on one side, formed by the long complementarity-determining region 1 of the light chain and the long complementarity-determining region 3 of the heavy chain, and has a cavity accommodating a glucose moiety. The model of the 19.1.2 site is basically flat with a shallow groove that can accommodate several internal glucose units. These results support the earlier conclusions, from ligand binding data, that W3129 has a cavity-type site, involving the terminal nonreducing glucose residue (endbinder), whereas 19.1.2 has a groove-type site.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19156207 S.L.Diaz, V.Padler-Karavani, D.Ghaderi, N.Hurtado-Ziola, H.Yu, X.Chen, E.C.Brinkman-Van der Linden, A.Varki, and N.M.Varki (2009).
Sensitive and specific detection of the non-human sialic Acid N-glycolylneuraminic acid in human tissues and biotherapeutic products.
  PLoS ONE, 4, e4241.  
18621718 B.Vulliez-Le Normand, F.A.Saul, A.Phalipon, F.Bélot, C.Guerreiro, L.A.Mulard, and G.A.Bentley (2008).
Structures of synthetic O-antigen fragments from serotype 2a Shigella flexneri in complex with a protective monoclonal antibody.
  Proc Natl Acad Sci U S A, 105, 9976-9981.
PDB codes: 3bz4 3c5s 3c6s
18669916 V.Padler-Karavani, H.Yu, H.Cao, H.Chokhawala, F.Karp, N.Varki, X.Chen, and A.Varki (2008).
Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease.
  Glycobiology, 18, 818-830.  
10582166 A.H.Lucas, and D.C.Reason (1999).
Polysaccharide vaccines as probes of antibody repertoires in man.
  Immunol Rev, 171, 89.  
  10225914 L.Hougs, L.Juul, A.Svejgaard, and T.Barington (1999).
Structural requirements of the major protective antibody to Haemophilus influenzae type b.
  Infect Immun, 67, 2503-2514.
PDB code: 1hou
9122216 S.L.Harris, L.Craig, J.S.Mehroke, M.Rashed, M.B.Zwick, K.Kenar, E.J.Toone, N.Greenspan, F.I.Auzanneau, J.R.Marino-Albernas, B.M.Pinto, and J.K.Scott (1997).
Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies.
  Proc Natl Acad Sci U S A, 94, 2454-2459.  
8766565 F.Brard, F.Jovelin, S.Petit, F.Tron, and D.Gilbert (1996).
Structural properties and mutation patterns of anti-nucleosome monoclonal antibodies are similar to those of anti-DNA antibodies.
  Eur J Immunol, 26, 1587-1594.  
  7622221 M.H.Nahm, K.H.Kim, P.Anderson, S.V.Hetherington, and M.K.Park (1995).
Functional capacities of clonal antibodies to Haemophilus influenzae type b polysaccharide.
  Infect Immun, 63, 2989-2994.  
7696844 A.Imberty, F.Casset, C.V.Gegg, M.E.Etzler, and S.Pérez (1994).
Molecular modelling of the Dolichos biflorus seed lectin and its specific interactions with carbohydrates: alpha-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide.
  Glycoconj J, 11, 400-413.  
8026889 I.Kawashima, M.Kotani, H.Ozawa, M.Suzuki, and T.Tai (1994).
Generation of monoclonal antibodies specific for ganglioside lactones: evidence of the expression of lactone on human melanoma cells.
  Int J Cancer, 58, 263-268.  
1377513 L.J.Nell, J.A.McCammon, and S.Subramaniam (1992).
Anti-insulin antibody structure and conformation. I. Molecular modeling and mechanics of an insulin antibody.
  Biopolymers, 32, 11-21.  
  1484268 R.A.Insel, E.E.Adderson, and W.L.Carroll (1992).
The repertoire of human antibody to the Haemophilus influenzae type b capsular polysaccharide.
  Int Rev Immunol, 9, 25-43.  
1286874 S.U.Shin, A.Wright, V.Bonagura, and S.L.Morrison (1992).
Genetically-engineered antibodies: tools for the study of diverse properties of the antibody molecule.
  Immunol Rev, 130, 87.  
  1717254 A.Wright, M.H.Tao, E.A.Kabat, and S.L.Morrison (1991).
Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure.
  EMBO J, 10, 2717-2723.  
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 codes are shown on the right.

 

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