Crystal structure analysis of full-length carboxyl-terminal Src kinase at 2.5 A resolutionCrystal structure analysis of full-length carboxyl-terminal Src kinase at 2.5 A resolution
Structural highlights
1k9a is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
CSK_RAT Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity).[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J Biol Chem. 1991 Dec 25;266(36):24249-52. PMID:1722201
↑Ruzzene M, James P, Brunati AM, Donella-Deana A, Pinna LA. Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and by polycationic effectors. J Biol Chem. 1994 Jun 3;269(22):15885-91. PMID:7515063
