Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution.
The three-dimensional crystal structure of the complex between the Fab from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme, has been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution. The antibody contacts the antigen with residues from all its complementarity determining regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant making hydrogen bonds and van der Waals interactions with the antibody. Water molecules at or near the antigen-antibody interface mediate some contacts between antigen and antibody. The fine specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can be explained on the basis of the refined model.
Fischmann
T O
TO
Département d'Immunologie, Institut Pasteur, Paris, France.
Bentley
G A
GA
Bhat
T N
TN
Boulot
G
G
Mariuzza
R A
RA
Phillips
S E
SE
Tello
D
D
Poljak
R J
RJ
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001666:Binding Sites, Antibody; D000939:Epitopes / Q000737:chemistry; D007140:Immunoglobulin Fab Fragments; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry / Q000276:immunology*; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007140:Immunoglobulin Fab Fragments; D009113:Muramidase