Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.
Chitarra, V, Alzari, P M, Bentley, G A, Bhat, T N, Eiselé, J L, Houdusse, A, ...
Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody...
Lascombe, M B, Alzari, P M, Poljak, R J, Nisonoff, A
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and...
Lascombe, M B, Alzari, P M, Boulot, G, Saludjian, P, Tougard, P, Berek, C, ...
The crystal structure of Fab R19.9, derived from an anti-p-azobenzenearsonate monoclonal antibody, has been determined and refined to 2.8-A resolution by x-ray crystallographic techniques. Monoclonal...
Amzel, L. M., Poljak, R. J., Saul, F., Varga, J. M., Richards, Frank F.
IgG New binds ligands such as orceine, menadione, and uridine with a low affinity (K0 about 1 × 103 liter/mol) and a γ-hydroxy derivative of vitamin K1 with a higher affinity (K0 = 1.7 × 105...
Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution
Poljak, R. J., Amzel, L. M., Avey, H. P., Chen, B. L., Phizackerley, R. P., Saul, F.
The structure of the Fab′ fragment of a human myeloma immunoglobulin was determined by x-ray crystallographic analysis at 2.8-Å resolution. The Fourier map of the electron density was correlated...
Poljak, R. J., Amzel, L. M., Chen, B. L., Phizackerley, R. P., Saul, F.
The structural analysis of the Fab′ fragment of human myeloma immunoglobulin IgGl(λ) New has been extended to a nominal resolution of 2.0 Å. Each of the structural subunits corresponding to the...
Bound water molecules and conformational stabilization help mediate an antigen-antibody association.
Bhat, T N, Bentley, G A, Boulot, G, Greene, M I, Tello, D, Dall'Acqua, W, ...
We report the three-dimensional structures, at 1.8-A resolution, of the Fv fragment of the anti-hen egg white lysozyme antibody D1.3 in its free and antigen-bound forms. These structures reveal a...
Alzari, P M, Spinelli, S, Mariuzza, R A, Boulot, G, Poljak, R J, Jarvis, J M, ...
The three-dimensional structure of the Fab fragment of an anti-2-phenyloxazolone monoclonal antibody (NQ10/12.5) in its native and complexed forms has been determined at 2.8 and 3.0 A resolution,...
Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.
Chitarra, V, Alzari, P M, Bentley, G A, Bhat, T N, Eiselé, J L, Houdusse, A, ...
Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody...
Lascombe, M B, Alzari, P M, Poljak, R J, Nisonoff, A
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and...
Lascombe, M B, Alzari, P M, Boulot, G, Saludjian, P, Tougard, P, Berek, C, ...
The crystal structure of Fab R19.9, derived from an anti-p-azobenzenearsonate monoclonal antibody, has been determined and refined to 2.8-A resolution by x-ray crystallographic techniques. Monoclonal...
Amzel, L. M., Poljak, R. J., Saul, F., Varga, J. M., Richards, Frank F.
IgG New binds ligands such as orceine, menadione, and uridine with a low affinity (K0 about 1 × 103 liter/mol) and a γ-hydroxy derivative of vitamin K1 with a higher affinity (K0 = 1.7 × 105...
Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution
Poljak, R. J., Amzel, L. M., Avey, H. P., Chen, B. L., Phizackerley, R. P., Saul, F.
The structure of the Fab′ fragment of a human myeloma immunoglobulin was determined by x-ray crystallographic analysis at 2.8-Å resolution. The Fourier map of the electron density was correlated...
Poljak, R. J., Amzel, L. M., Chen, B. L., Phizackerley, R. P., Saul, F.
The structural analysis of the Fab′ fragment of human myeloma immunoglobulin IgGl(λ) New has been extended to a nominal resolution of 2.0 Å. Each of the structural subunits corresponding to the...
Bound water molecules and conformational stabilization help mediate an antigen-antibody association.
Bhat, T N, Bentley, G A, Boulot, G, Greene, M I, Tello, D, Dall'Acqua, W, ...
We report the three-dimensional structures, at 1.8-A resolution, of the Fv fragment of the anti-hen egg white lysozyme antibody D1.3 in its free and antigen-bound forms. These structures reveal a...
Alzari, P M, Spinelli, S, Mariuzza, R A, Boulot, G, Poljak, R J, Jarvis, J M, ...
The three-dimensional structure of the Fab fragment of an anti-2-phenyloxazolone monoclonal antibody (NQ10/12.5) in its native and complexed forms has been determined at 2.8 and 3.0 A resolution,...