Three-dimensional structure and antigen binding specificity of antibodies.
A number of specific Fab and Fv fragments and their complexes with antigens (avian lysozymes), haptens, and anti-idiotopic Fabs have been studied by immunochemical and crystallographic techniques. Antigen and antibody interact through closely complementary contacting surfaces, without major conformational changes. An idiotopic determinant of a monoclonal antibody is shown to include parts of most of its complementarity determining regions. The specificity of antigen recognition resides in the close complementarity of the antigenic determinant with the antibody combining site.
Tello
D
D
URA 359 CNRS, Department of Immunology, Institut Pasteur, Paris, France.
Spinelli
S
S
Souchon
H
H
Saul
F A
FA
Riottot
M M
MM
Mariuzza
R A
RA
Lascombe
M B
MB
Houdusse
A
A
Eiselé
J L
JL
Fischmann
T
T
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000915:Antibody Affinity; D000918:Antibody Specificity; D000939:Epitopes; D006241:Haptens / Q000276:immunology; D006822:Hybrid Cells / Q000276:immunology; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D007130:Immunoglobulin Idiotypes / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D009113:Muramidase / Q000737:chemistry / Q000276:immunology*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000911:Antibodies, Monoclonal; D000939:Epitopes; D006241:Haptens; D007140:Immunoglobulin Fab Fragments; D007130:Immunoglobulin Idiotypes; D009113:Muramidase