Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specia...
Main Authors: | Filippakopoulos, P, Kofler, M, Hantschel, O, Gish, G, Grebien, F, Salah, E, Neudecker, P, Kay, L, Turk, B, Superti-Furga, G, Pawson, T, Knapp, S |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2008
|
Similar Items
-
Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
by: Filippakopoulos, P, et al.
Published: (2008) -
SH2 domains: modulators of nonreceptor tyrosine kinase activity.
by: Filippakopoulos, P, et al.
Published: (2009) -
Small-molecule inhibitors of the c-Fes protein-tyrosine kinase.
by: Hellwig, S, et al.
Published: (2012) -
Structure and substrate specificity of the Pim-1 kinase
by: Bullock, A, et al.
Published: (2005) -
Structure and substrate specificity of the Pim-1 kinase.
by: Bullock, A, et al.
Published: (2005)