1CSZ
SYK TYROSINE KINASE C-TERMINAL SH2 DOMAIN COMPLEXED WITH A PHOSPHOPEPTIDEFROM THE GAMMA CHAIN OF THE HIGH AFFINITY IMMUNOGLOBIN G RECEPTOR, NMR
Summary for 1CSZ
Entry DOI | 10.2210/pdb1csz/pdb |
Descriptor | SYK PROTEIN TYROSINE KINASE, ACETYL-THR-PTR-GLU-THR-LEU-NH2 (2 entities in total) |
Functional Keywords | protein-tyrosine kinase sh2 domain, complex (phosphotransferase-peptide), complex (phosphotransferase-peptide) complex, complex (phosphotransferase/peptide) |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 13464.36 |
Authors | Narula, S.S.,Yuan, R.W.,Adams, S.E.,Green, O.M.,Green, J.,Phillips, T.B.,Zydowsky, L.D.,Botfield, M.C.,Hatada, M.H.,Laird, E.R.,Zoller, M.J.,Karas, J.L.,Dalgarno, D.C. (deposition date: 1995-10-03, release date: 1996-11-08, Last modification date: 2024-10-30) |
Primary citation | Narula, S.S.,Yuan, R.W.,Adams, S.E.,Green, O.M.,Green, J.,Philips, T.B.,Zydowsky, L.D.,Botfield, M.C.,Hatada, M.,Laird, E.R.,Zoller, M.J.,Karas, J.L.,Dalgarno, D.C. Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide. Structure, 3:1061-1073, 1995 Cited by PubMed Abstract: 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: 8590001DOI: 10.1016/S0969-2126(01)00242-8 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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