rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2002-6-13
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pubmed:abstractText |
Site-selective dephosphorylation of receptor tyrosine kinases contributes to receptor regulation. The receptor-like protein tyrosine phosphatase DEP-1 site-selectively dephosphorylates the PDGF beta-receptor. DEP-1 dephosphorylation of original and chimeric phospho-peptides spanning the preferred pY1021 and the less preferred pY857 and pY562 sites was analyzed. Double substitutions of basic residues at -4 and +3 of pY857 and pY562 peptides improved affinity. Substitutions of single amino acids indicated preference for an acidic residue at position -1 and a preference against a basic residue at position +3. DEP-1 site-selective dephosphorylation of PDGF beta-receptor is thus determined by the primary sequence surrounding phosphorylation sites and involves interactions with residues spanning at least between positions -1 and +3.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
517
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12062403-Alanine,
pubmed-meshheading:12062403-Amino Acid Sequence,
pubmed-meshheading:12062403-Amino Acid Substitution,
pubmed-meshheading:12062403-Catalytic Domain,
pubmed-meshheading:12062403-Kinetics,
pubmed-meshheading:12062403-Lysine,
pubmed-meshheading:12062403-Molecular Sequence Data,
pubmed-meshheading:12062403-Phosphopeptides,
pubmed-meshheading:12062403-Phosphorylation,
pubmed-meshheading:12062403-Protein Tyrosine Phosphatases,
pubmed-meshheading:12062403-Receptor, Platelet-Derived Growth Factor beta,
pubmed-meshheading:12062403-Receptor-Like Protein Tyrosine Phosphatases, Class 3,
pubmed-meshheading:12062403-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1.
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pubmed:affiliation |
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
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pubmed:publicationType |
Journal Article
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