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1YQV

The crystal structure of the antibody Fab HyHEL5 complex with lysozyme at 1.7A resolution

Replaces:  3HFLReplaces:  2HFL
Summary for 1YQV
Entry DOI10.2210/pdb1yqv/pdb
DescriptorHyHEL-5 Antibody Light Chain, HyHEL-5 Antibody Heavy Chain, Hen Egg White Lysozyme, ... (4 entities in total)
Functional Keywordshyhel-5 antibody, lysozyme, immune system
Biological sourceMus musculus (house mouse)
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Cellular locationSecreted: P00698
Total number of polymer chains3
Total formula weight60588.38
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 citationCohen, 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: 15858274
DOI: 10.1107/S0907444905007870
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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