Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization
Article Abstract:
Dimerization and active-site blockage inhibit receptor-like protein-tyrosine phosphatase-alpha (RPTP-alpha) activity. The membrane-proximal catalytic domain (D1) of murine RPTP-alpha (RPTP-alpha-D1) has helix-turn-helix structure at the amino-terminal and a two-stranded beta-sheet between residues 211 to 213 and 458 to 461. In RPTP-alpha-D1 dimer, the helix-turn-helix structure is inserted into the active site of the opposing monomer. This makes the RPTP-alpha-D1 dimer catalytically inactive as it is incapable of binding to its substrates.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase
Article Abstract:
A new complementary DNA (cDNA) corresponding to a messenger RNA that can be induced by oxidative stress and heat shock in human skin cells has been purified and analysed. The cDNA carries the genetic information for a protein with a strong structural resemblance to a non-receptor-type protein-tyrosine phosphatase. The induction of this gene may influence human cellular response to environmental pressure caused by toxic oxidants.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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A plant oncogene as a phosphatase
Article Abstract:
RolB protein overproduced in Escherichia coli has tyrosine phosphatase activity. Differentiation and growth of neoplastic roots in dicotyledonous plants appears to be induced by the plant oncogene rolB, from Agrobacterium rhizogenes. An increased membrane sensitivity to the plant hormone auxin is found in rolB-transformed plant cells.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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