The tyrosine kinase Csk dimerizes through its SH3 domain
Nicholas M. Levinson, Patrick R. Visperas and John Kuriyan
Figure 1. - The SH3 domain of Csk is required for dimerization
A) The constructs used in this paper. B) The results of size exclusion chromatography performed with the constructs shown in A. The elution volumes of molecular weight standards are indicated by black arrows.
Figure 2. - The Csk SH3-SH3 dimer A) A representative SH3-SH3 dimer from the crystal structure of full-length Csk (PDB code: 1K9A). Residues in the interface are highlighted. B) The results of size exclusion chromatography performed with constructs of Csk bearing mutations in the putative dimer interface.
Figure 3. - The Csk SH3-SH3 dimer is incompatible with the binding of ligands to the SH3 domain The solution structure of the SH3 domain of Csk in complex with the phosphatase-derived peptide PEP-3BP1 (pdb code 1JEG). The residues of Csk that are involved in the SH3-SH3 dimer interface are highlighted by sticks and black dots as in figure 2.