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http://purl.uniprot.org/citations/12482860http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12482860http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12482860http://www.w3.org/2000/01/rdf-schema#comment"SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a negative regulator in eukaryotic cellular signaling pathways. To understand its regulatory mechanism, we have determined the crystal structure of the C-terminal truncated human SHP-1 in the inactive conformation at 2.8-A resolution and refined the structure to a crystallographic R-factor of 24.0%. The three-dimensional structure shows that the ligand-free SHP-1 has an auto-inhibited conformation. Its N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, which supports that the phosphatase activity of SHP-1 is primarily regulated by the N-SH2 domain. In addition, the C-SH2 domain of SHP-1 has a different orientation from and is more flexible than that of SHP-2, which enables us to propose an enzymatic activation mechanism in which the C-SH2 domains of SHPs could be involved in searching for phosphotyrosine activators."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210430200"xsd:string
http://purl.uniprot.org/citations/12482860http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210430200"xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Liang X."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Liang X."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Song X."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Song X."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"He D."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"He D."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Zhou G.W."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Zhou G.W."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Zhao Z.J."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/author"Zhao Z.J."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/pages"6516-6520"xsd:string
http://purl.uniprot.org/citations/12482860http://purl.uniprot.org/core/pages"6516-6520"xsd:string