Protein Engineering, Vol. 12, No. 2, 129-139,
February 1999
© 1999 Oxford University Press
Molecular dynamics simulation of 
-lactalbumin and calcium binding c-type lysozyme
Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, Division of Biological Sciences, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA
-Lactalbumins (LAs) and c-type lysozymes (LYZs) are two classes of proteins which have a 35–40% sequence homology and share a common three dimensional fold but perform different functions. Lysozymes bind and cleave the glycosidic bond linkage in sugars, where as, -lactalbumin does not bind sugar but participates in the synthesis of lactose. -Lactalbumin is a metallo-protein and binds calcium, where as, only a few of the LYZs bind calcium. These proteins consist of two domains, an -helical and a ß-strand domain, separated by a cleft. Calcium is bound at a loop situated at the bottom of the cleft and is important for the structural integrity of the protein. Calcium is an ubiquitous intracellular signal in higher eukaryotes and structural changes induced on calcium binding have been observed in a number of proteins. In the present study, molecular dynamics simulations of equine LYZ and human LA, with and without calcium, were carried out. We detail the differences in the dynamics of equine LYZ and human LA, and discuss it in the light of experimental data already available and relate it to the behavior of the functionally important regions of both the proteins. These simulations bring out the role of calcium in the conformation and dynamics of these metallo-proteins. In the calcium bound LA, the region of the protein around the calcium binding site is not only frozen but the atomic fluctuations are found to increase away from the binding site and peak at the exposed sites of the protein. This channeling of fluctuations away from the metal binding site could serve as a general mechanism by which the effect of metal binding at a site is transduced to other parts of the protein and could play a key role in protein–ligand and/or protein–protein interaction.
Keywords: calcium-binding proteins/lactose synthase/c-type lysozyme/atomic fluctuations/functionally important motion
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