1JHL

THREE-DIMENSIONAL STRUCTURE OF A HETEROCLITIC ANTIGEN-ANTIBODY CROSS-REACTION COMPLEX

Summary for 1JHL

• Entry DOI: 10.2210/pdb1jhl/pdb
• Descriptor: IGG1-KAPPA D11.15 FV (LIGHT CHAIN), IGG1-KAPPA D11.15 FV (HEAVY CHAIN), PHEASANT EGG WHITE LYSOZYME (3 entities in total)
• Functional Keywords: complex(antibody-antigen)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Secreted: P00702
• Total number of polymer chains: 3
• Total formula weight: 39121.69

Authors

Chitarra, V.,Alzari, P.M.,Bentley, G.A.,Bhat, T.N.,Eisele, J.-L.,Poljak, R.J. (deposition date: 1993-05-04, release date: 1994-01-31, Last modification date: 2024-10-09)

Primary citation

Chitarra, V.,Alzari, P.M.,Bentley, G.A.,Bhat, T.N.,Eisele, J.L.,Houdusse, A.,Lescar, J.,Souchon, H.,Poljak, R.J.
Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.
Proc.Natl.Acad.Sci.USA, 90:7711-7715, 1993

PubMed Abstract: 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 (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the crystal structure of the Fv fragment of D11.15 complexed with pheasant egg lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in the affinity of D11.15 for the lysozymes appear to result from sequence substitutions in these antigens at the interface with the antibody. More generally, cross-reactivity is seen to require a stereochemically permissive environment for the variant antigen residues at the antibody-antigen interface.

PubMed: 8356074
DOI: 10.1073/pnas.90.16.7711

Experimental method

X-RAY DIFFRACTION (2.4 Å)