Article
Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src.
Nature structural biology - 1 Apr 2000
Gonfloni S, Weijland A, Kretzschmar J, Superti-Furga G
Abstract excerpt
The catalytic activity of Src family tyrosine kinases is inhibited by intramolecular interactions between the regulatory SH3 and SH2 domains and the catalytic domain. In the inactive state, the critical alphaC-helix in the catalytic domain is positioned such that the formation of the Glu 310-Lys 295 salt bridge is precluded, Tyr 416 in the activation loop is unphosphorylated, and the SH2 and SH3 domains are...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Binding Sites
- Catalytic Domain
- Cell Line
- Chickens
- Enzyme Activation
- Feedback
- Humans
- Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
- Models, Molecular
- Mutation
- Peptides
- Phosphorylation
- Phosphotyrosine
- Protein Structure, Secondary
- Proto-Oncogene Proteins pp60(c-src)