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1yqv

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Image:1yqv.gif

1yqv, resolution 1.7Å

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

Overview

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.

About this Structure

1YQV is a Single protein structure of sequence from Gallus gallus and Mus musculus. This structure superseeds the now removed PDB entries 3HFL and 2HFL. The following page contains interesting information on the relation of 1YQV with [Antibodies]. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

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., Cohen GH, Silverton EW, Padlan EA, Dyda F, Wibbenmeyer JA, Willson RC, Davies DR, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):628-33. Epub 2005, Apr 20. PMID:15858274

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