A new flavor in phosphotyrosine recognition.
The phosphotyrosine-binding (PTB) domain, recently identified in a number of proteins, specifically recognizes tyrosine-phosphorylated sequences in other proteins. Although similar in function to the well-studied SH2 domain, the PTB domain appears to be structurally unrelated.
Eck
M J
MJ
Department of Medicine, Children's Hospital, Boston, MA 02115, USA.
D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D019000:Phosphotyrosine; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism
D001798:Blood Proteins; D010750:Phosphoproteins; D011956:Receptors, Cell Surface; C039077:platelet protein P47; D019000:Phosphotyrosine; D014443:Tyrosine; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)