|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1996-3-28
|
|
pubmed:abstractText |
Recruitment of the intracellular tyrosine kinase Syk to activated immune-response receptors is a critical early step in intracellular signaling. In mast cells, Syk specifically associates with doubly phosphorylated immunoreceptor tyrosine-based activation motifs (ITAMs) that are found within the IgE receptor. The mechanism by which Syk recognizes these motifs is not fully understood. Both Syk SH2 (Src homology 2) domains are required for high-affinity binding to these motifs, but the C-terminal SH2 domain (Syk-C) can function independently and can bind, in isolation, to the tyrosine-phosphorylated IgE receptor in vitro. In order to improve understanding of the cellular function of Syk, we have determined the solution structure of Syk-C complexed with a phosphotyrosine peptide derived from the gamma subunit of the IgE receptor.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP70 protein, human
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0969-2126
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
3
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
N
|
|
pubmed:pagination |
1061-73
|
|
pubmed:dateRevised |
2011-11-2
|
|
pubmed:meshHeading |
pubmed-meshheading:8590001-Amino Acid Sequence,
pubmed-meshheading:8590001-Binding Sites,
pubmed-meshheading:8590001-Enzyme Precursors,
pubmed-meshheading:8590001-Humans,
pubmed-meshheading:8590001-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8590001-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8590001-Models, Molecular,
pubmed-meshheading:8590001-Molecular Sequence Data,
pubmed-meshheading:8590001-Phosphopeptides,
pubmed-meshheading:8590001-Phosphotyrosine,
pubmed-meshheading:8590001-Protein Conformation,
pubmed-meshheading:8590001-Protein-Tyrosine Kinases,
pubmed-meshheading:8590001-Receptors, IgE,
pubmed-meshheading:8590001-Sequence Homology, Amino Acid,
pubmed-meshheading:8590001-Software,
pubmed-meshheading:8590001-ZAP-70 Protein-Tyrosine Kinase,
pubmed-meshheading:8590001-src Homology Domains
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide.
|
|
pubmed:affiliation |
Ariad Pharmaceuticals Inc., Cambridge, MA 02139, USA.
|
|
pubmed:publicationType |
Journal Article
|
