1jtp
Degenerate interfaces in antigen-antibody complexes
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| , resolution 1.9Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Related: | 1MEL, 1JTO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1JTP is a Protein complex structure of sequences from Camelus dromedarius and Meleagris gallopavo. Full crystallographic information is available from OCA.
ReferenceReference
Degenerate interfaces in antigen-antibody complexes., Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L, J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532
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