1FDL

CRYSTALLOGRAPHIC REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURE OF THE FAB D1.3-LYSOZYME COMPLEX AT 2.5-ANGSTROMS RESOLUTION

Summary for 1FDL

• Entry DOI: 10.2210/pdb1fdl/pdb
• Descriptor: IGG1-KAPPA D1.3 FAB (LIGHT CHAIN), IGG1-KAPPA D1.3 FAB (HEAVY CHAIN), HEN EGG WHITE LYSOZYME (3 entities in total)
• Functional Keywords: complex (antibody-antigen)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 3
• Total formula weight: 61406.46

Authors

Fischmann, T.O.,Poljak, R.J. (deposition date: 1990-08-27, release date: 1991-10-15, Last modification date: 2024-11-20)

Primary citation

Fischmann, T.O.,Bentley, G.A.,Bhat, T.N.,Boulot, G.,Mariuzza, R.A.,Phillips, S.E.,Tello, D.,Poljak, R.J.
Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution.
J.Biol.Chem., 266:12915-12920, 1991

PubMed Abstract: 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.

PubMed: 1712773

Experimental method

X-RAY DIFFRACTION (2.5 Å)