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Solvent rearrangement in an antigen-antibody interface introduced by site-directed mutagenesis of the antibody combining site.

Abstract：

:The three-dimensional structure of a site-directed mutant of the bacterially expressed Fv fragment from monoclonal antibody D1.3, complexed to the specific antigen lysozyme has been determined to a nominal resolution of 1.8 A using X-ray diffraction data. The replacement of VL Trp92 by Asp allows two water molecules to occupy space taken by Trp92 in the wild-type complex, in agreement with a previous observation that water molecules play an important role in stabilizing this antigen-antibody complex. The equilibrium constant for the binding of the mutant Fv to the antigen decreases by three orders of magnitude (from 2.3 x 10(8) M-1 to 2.6 x 10(5) M-1). Titration calorimetry shows that this results from a smaller negative binding enthalpy (delta delta H = -16 kJ mol-1 at 24 degrees C), whereas the value of the binding entropy is not affected. Since in the complex between the mutated Fv and antigen the buried area has decreased relative to that of the wild-type Fv by about 150 A2, the contribution of the buried unit area to the decrease in free energy (delta Gzero) is approximately 117 J mol-1 (28 cal mol-1) per A2. The loss of interatomic contacts in replacing Trp by Asp permits an approximate calculation for the contribution of van der Waals interactions made by Trp92 in this complex, which gives an average of 2.1 kJ mol-1 (0.5 kcal mol-1) for contacts between carbon atoms.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ysern X,Fields BA,Bhat TN,Goldbaum FA,Dall'Acqua W,Schwarz FP,Poljak RJ,Mariuzza RA

doi

10.1006/jmbi.1994.1309

subject

Has Abstract

pub_date

1994-05-13 00:00:00

pages

496-500

issue

4

eissn

0022-2836

issn

1089-8638

journal_volume

238

pub_type

杂志文章

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