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Prediction of Three-Dimensional Structures of Enzyme-Substrate and Enzyme-Inhibitor Complexes of Lysozyme
Matthew R. Pincus, S. Scott Zimmerman and Harold A. Scheraga
Proceedings of the National Academy of Sciences of the United States of America
Vol. 73, No. 12 (Dec., 1976), pp. 4261-4265
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/66088
Page Count: 5
You can always find the topics here!Topics: Active sites, Enzymes, Molecules, Atoms, Geometric angles, Enzyme substrates, Disaccharides, Rigid structures, Energy value, Dimers
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Conformational energy calculations were used to predict the three-dimensional structures of enzyme-substrate and enzyme-inhibitor complexes of lysozyme. A global search method, involving the use of a disaccharide fragment molecule, was used initially to determine all favorable binding regions at the active site. It is shown that the binding of a series of (nonfragmented) oligomers of N-acetylglucosamine is highly specific. The results show further that (a) theenzyme recognizes only one backbone conformation of the oligomer, corresponding to a left-handed helix, and (b) for saccharides containing two or more N-acetylglucosamine residues, two residues bind preferentially to the C and D sites. The calculations also suggest that the chair form of N-acetylglucosamine can bind to the D region. The saccharide residues of tetra-N-acetylglucosamine bind to the A-B-C-D sites, with the residues at the A-B-C sites having essentially the same conformation and orientation as those in the x-ray structure of tetra-N-acetylglucosamine-δ -lactone bound to lysozyme.
Proceedings of the National Academy of Sciences of the United States of America © 1976 National Academy of Sciences