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(Received for publication, August 22, 1996, and in revised form, September 20, 1996)
From the Department of Cell and Molecular Biology, Northwestern
University Medical School, and the Northwestern University
Institute for Neuroscience, Chicago, Illinois 60611-3008
The epitope on tau protein recognized by the
monoclonal antibody Alz50 was defined through internal deletion
mutagenesis and quantified by affinity measurements. The epitope is
discontinuous and requires both a previously identified N-terminal
segment and the microtubule binding region for efficient binding of
Alz50. The interaction between these regions is consistent with an
intramolecular reaction mechanism, suggesting that Alz50 binding
depends on the conformation of individual tau monomers. The results
suggest that tau adopts a distinct conformation when polymerized into
filaments and that this conformation is recognized selectively by
Alz50.
Volume 271, Number 51,
Issue of December 20, 1996
pp. 32789-32795
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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