1JTO

Degenerate interfaces in antigen-antibody complexes

Summary for 1JTO

• Entry DOI: 10.2210/pdb1jto/pdb
• Related: 1MEL
• Descriptor: Vh Single-Domain Antibody, Lysozyme (3 entities in total)
• Functional Keywords: immunoglobulin, heavy chain antibody, vhh, interface, antibody, hydrolase
• Biological source: Camelus dromedarius (Arabian camel); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 4
• Total formula weight: 59976.50

Authors

Decanniere, K.,Transue, T.R.,Desmyter, A.,Maes, D.,Muyldermans, S.,Wyns, L. (deposition date: 2001-08-21, release date: 2001-10-31, Last modification date: 2024-10-30)

Primary citation

Decanniere, K.,Transue, T.R.,Desmyter, A.,Maes, D.,Muyldermans, S.,Wyns, L.
Degenerate interfaces in antigen-antibody complexes.
J.Mol.Biol., 313:473-478, 2001

PubMed Abstract: In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.

PubMed: 11676532
DOI: 10.1006/jmbi.2001.5075

Experimental method

X-RAY DIFFRACTION (2.5 Å)