3HFM

STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX

Summary for 3HFM

• Entry DOI: 10.2210/pdb3hfm/pdb
• Descriptor: HYHEL-10 IGG1 FAB (LIGHT CHAIN), HYHEL-10 IGG1 FAB (HEAVY CHAIN), HEN EGG WHITE LYSOZYME, ... (4 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: 61206.89

Authors

Padlan, E.A.,Davies, D.R. (deposition date: 1988-08-11, release date: 1989-07-12, Last modification date: 2024-11-20)

Primary citation

Padlan, E.A.,Silverton, E.W.,Sheriff, S.,Cohen, G.H.,Smith-Gill, S.J.,Davies, D.R.
Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex.
Proc.Natl.Acad.Sci.USA, 86:5938-5942, 1989

PubMed Abstract: The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence. It consists of the exposed residues of an alpha-helix together with surrounding amino acids. The epitope crosses the active-site cleft and includes a tryptophan located within this cleft. The combining site of the antibody is mostly flat with a protuberance made up of two tyrosines that penetrate the cleft. All six complementarity-determining regions of the Fab contribute at least one residue to the binding; one residue from the framework is also in contact with the lysozyme. The contacting residues on the antibody contain a disproportionate number of aromatic side chains. The antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions; there is one ion-pair interaction but it is weak.

PubMed: 2762305
DOI: 10.1073/pnas.86.15.5938

Experimental method

X-RAY DIFFRACTION (3 Å)