Water molecules in the antibody–antigen interface of the structure of the Fab HyHEL-5–lysozyme complex at 1.7 Å resolution: comparison with results from isothermal titration calorimetry
| Autor: | Enid W. Silverton, G. H. Cohen, Fred Dyda, David R. Davies, Jamie A. Wibbenmeyer, Eduardo A. Padlan, Richard C. Willson |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Quality Control Protein Conformation Recombinant fab Complex formation Resolution (electron density) Water Isothermal titration calorimetry Antigen-Antibody Complex General Medicine Crystal structure Calorimetry Crystallography X-Ray Epitopes chemistry.chemical_compound Crystallography chemistry Structural Biology Antibody antigen Molecule Muramidase Cloning Molecular Lysozyme |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 61:628-633 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444905007870 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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