1YQV
The crystal structure of the antibody Fab HyHEL5 complex with lysozyme at 1.7A resolution
Replaces: 3HFLReplaces: 2HFLSummary for 1YQV
Entry DOI | 10.2210/pdb1yqv/pdb |
Descriptor | HyHEL-5 Antibody Light Chain, HyHEL-5 Antibody Heavy Chain, Hen Egg White Lysozyme, ... (4 entities in total) |
Functional Keywords | hyhel-5 antibody, lysozyme, immune system |
Biological source | Mus musculus (house mouse) More |
Cellular location | Secreted: P00698 |
Total number of polymer chains | 3 |
Total formula weight | 60588.38 |
Authors | Cohen, G.H.,Silverton, E.W.,Padlan, E.A.,Dyda, F.,Wibbenmeyer, J.A.,Wilson, R.C.,Davies, D.R. (deposition date: 2005-02-02, release date: 2005-04-26, Last modification date: 2024-10-30) |
Primary citation | Cohen, G.H.,Silverton, E.W.,Padlan, E.A.,Dyda, F.,Wibbenmeyer, J.A.,Willson, R.C.,Davies, D.R. Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 A resolution: comparison with results from isothermal titration calorimetry. Acta Crystallogr.,Sect.D, 61:628-633, 2005 Cited by PubMed Abstract: The structure of the complex between hen egg-white lysozyme and the Fab HyHEL-5 at 2.7 A resolution has previously been reported [Cohen et al. (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant Fab, the X-ray structure of the complex has been re-evaluated at 1.7 A resolution. The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. The model of the full complex has improved significantly, yielding an R(work) of 19.5%. With this model, the structural results can be compared with the results of isothermal titration calorimetry. An attempt has been made to estimate the changes in bound waters that accompany complex formation and the difficulties inherent in using the crystal structures to provide the information necessary to make this calculation are discussed. PubMed: 15858274DOI: 10.1107/S0907444905007870 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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