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Intramolecular interactions in protein tyrosine phosphatase RPTPmu: kinetic evidence.

Abstract:

The receptor-like protein tyrosine phosphatase RPTPmu contains three intracellular domains: the juxtamembrane (JM) and two phosphatase domains (D1 and D2). D1 is catalytically active in vitro. The functional roles of JM and D2 are still unclear. To find out whether and how they modulate the phosphatase activity of D1, we compared the enzymatic characteristics of two constructs, containing a truncated JM and either D1 or both phosphatase domains. p-Nitrophenyl phosphate and two peptide substra...

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Publication status:
Published

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Publisher copy:
10.1006/bbrc.2000.4094

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, RDM, Molecular Medicine
Role:
Author
Journal:
Biochemical and biophysical research communications
Volume:
280
Issue:
1
Pages:
319-327
Publication date:
2001-01-05
DOI:
EISSN:
1090-2104
ISSN:
0006-291X
URN:
uuid:78c42a4b-1f60-48ec-bfd6-17303c7518c1
Source identifiers:
9163
Local pid:
pubs:9163

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