Literature DB >> 9757831

Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.

M J Wishart1, J E Dixon.   

Abstract

The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.

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Year:  1998        PMID: 9757831     DOI: 10.1016/s0968-0004(98)01241-9

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  47 in total

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