2004/03/25 by Anthony Mittermaier, Lewis E. Kay · 1 voice
Biochemistry, Genetics and Molecular Biology · Materials Science · #Enzyme Structure and Function #Protein Kinase Regulation and GTPase Signaling #Protein Structure and Dynamics
paper · pdf · doi:10.1110/ps.03502504
openalex publication_date 2004/03/25 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
We have used (15)N- and (2)H-NMR spin relaxation experiments to study the response of backbone and side-chain dynamics when a leucine or valine is substituted for a completely buried phenylalanine residue in the SH3 domain from the Fyn tyrosine kinase. Several residues show differences in the time scales and temperature dependences of internal motions when data for the three proteins are compared. Changes were also observed in the magnitude of dynamics, with the valine, and to a lesser extent leucine mutant, showing enhanced flexibility compared to the wild-type (WT) protein. The motions of many of the same amide and methyl groups are affected by both mutations, identifying a set of loci where dynamics are sensitive to interactions involving the targeted side chain. These results show that contacts within the hydrophobic core affect many aspects of internal mobility throughout the Fyn SH3 domain.