Literature summary for 2.7.10.2 extracted from

Futterer, K.; Wong, J.; Grucza, R.A.; Chan, A.C.; Waksman, G.
Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide (1998), J. Mol. Biol., 281, 523-537.

Search for more literature for 2.7.10.2

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the tandem SH2 domain of Syk complexed with a dually phosphorylated ITAM peptide. The structure is solved by multiple isomorphous replacement at 3.0 A resolution	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P43405	-	-

Synonyms

Synonyms	Comment	Organism
tyrosine-protein kinase SYK	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)