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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 DOI10.2210/pdb1csz/pdb
DescriptorSYK PROTEIN TYROSINE KINASE, ACETYL-THR-PTR-GLU-THR-LEU-NH2 (2 entities in total)
Functional Keywordsprotein-tyrosine kinase sh2 domain, complex (phosphotransferase-peptide), complex (phosphotransferase-peptide) complex, complex (phosphotransferase/peptide)
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight13464.36
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 citationNarula, 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: 8590001
DOI: 10.1016/S0969-2126(01)00242-8
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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