ATP:protein-tyrosine O-phosphotransferase (ambiguous)
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-141.
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-140 IN COMPLEX WITH NEF.
Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects.
The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.
Solution structure and peptide binding of the SH3 domain from human Fyn.
The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28.
The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
Dot far-western blot analysis of relative binding affinities of the Src homology 3 domains of Efs and its related proteins.
Nef proteins of distinct HIV-1 or -2 isolates differ in their binding properties for HCK: isolation of a novel Nef binding factor with characteristics of an adaptor protein.
Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation.
Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions.
HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution.
The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases.
A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.
SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn.
Binding of SAP SH2 domain to FynT SH3 domain reveals a novel mechanism of receptor signalling in immune regulation.
The E.C. was transferred from 2.7.1.112 to 2.7.10.2. ADP/ATP could be compatible with other Nucleoside diphosphate/Nucleoside triphosphate. This enzyme is composed of SH3 domain, SH2 domain and protein kinase domain. Although the structures of SH3 and SH2 domains have been determined, the catalytic domain of this enzyme has not been solved.