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(Received for publication, July 8, 1997, and in revised form, September 3, 1997)
,
From the Receptor-like protein-tyrosine phosphatases
(RPTPs) play important roles in regulating intracellular processes.
We have been investigating the regulation and function of RPTPµ, a
receptor-like PTP related to the Ig superfamily of cell adhesion
molecules. Recently, the crystal structure of a dimer of the membrane
proximal domain of RPTP
Laboratory of Molecular Biophysics,
University of Oxford, Rex Richards Building, South Parks Road, Oxford
OX1 3QU, United Kingdom and the ¶ Cold Spring Harbor Laboratory,
P. O. Box 100, Cold Spring Harbor, New York 11724
(RPTP D1) was described (Bilwes, A. M., den Hertog, J., Hunter, T., and Noel J. P. (1996)
Nature 382, 555-559). Within this crystal structure, the
catalytic site of each subunit of the dimer is sterically blocked by
the insertion of the N-terminal helix-turn-helix segment of the
dyad-related monomer. It was proposed that dimerization would lead to
inhibition of catalytic activity and may provide a paradigm for the
regulation of the RPTP family. We have determined the crystal
structure, to 2.3 Å resolution, of RPTPµ D1, which shares 46%
sequence identity with that of RPTP D1. Although the tertiary
structures of RPTP D1 and RPTPµ D1 are very similar, with a root
mean square deviation between equivalent C atoms of 1.1 Å, the
quaternary structures of these two proteins are different. Neither the
catalytic site nor the N-terminal helix-turn-helix segment of RPTPµ
D1 participates in protein-protein interactions. The catalytic site of
RPTPµ D1 is unhindered and adopts an open conformation similar to
that of the cytosolic PTP, PTP1B (Barford, D., Flint, A. J., and
Tonks, N. K. (1994) Science 263, 1397-1404). We
propose that dimerization-induced modulation of RPTP activity may not
be a general feature of this family of enzymes.
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