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The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu

K M Hoffmann1, N K Tonks, D Barford

  • 1Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom.

The Journal of Biological Chemistry
|November 5, 1997
PubMed

Insights

Receptor-like protein-tyrosine phosphatases (RPTPs) are crucial for cell processes. Structural analysis of RPTPmu reveals its catalytic site is unhindered, differing from RPTPalpha and suggesting varied regulation in the RPTP family.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Signaling

Background:

  • Receptor-like protein-tyrosine phosphatases (RPTPs) are key regulators of intracellular signaling pathways.
  • RPTPmu, related to Ig superfamily cell adhesion molecules, is under investigation for its regulatory mechanisms.
  • Previous studies on RPTPalpha suggested dimerization inhibits catalytic activity, potentially a common regulatory paradigm for RPTPs.

Purpose of the Study:

  • To determine the crystal structure of the membrane proximal domain of RPTPmu (RPTPmu D1).
  • To compare the quaternary structure of RPTPmu D1 with RPTPalpha D1.
  • To elucidate the regulatory mechanisms of RPTPmu and assess the generality of dimerization-induced inhibition in RPTPs.

Main Methods:

  • X-ray crystallography to determine the 2.3 Å resolution structure of RPTPmu D1.
  • Structural comparison of RPTPmu D1 and RPTPalpha D1, including tertiary and quaternary structures.
  • Analysis of protein-protein interactions and catalytic site accessibility in RPTPmu D1.

Main Results:

  • The crystal structure of RPTPmu D1 was determined at 2.3 Å resolution.
  • RPTPmu D1 shares high tertiary structural similarity with RPTPalpha D1 but exhibits distinct quaternary structures.
  • Unlike RPTPalpha D1, RPTPmu D1's catalytic site and N-terminal segment are not involved in protein-protein interactions, remaining unhindered and open.

Conclusions:

  • Dimerization-induced inhibition of catalytic activity may not be a universal regulatory mechanism for all RPTPs.
  • RPTPmu exhibits a unique structural arrangement potentially leading to different regulatory pathways compared to RPTPalpha.
  • Further research is needed to fully understand the diverse regulatory strategies within the RPTP family.

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