Article
Identification of a PU.1-IRF4 protein interaction surface predicted by chemical exchange line broadening.
Proceedings of the National Academy of Sciences of the United States of America - 21 Jan 2003
McKercher Scott R, Lombardo Christian R, Bobkov Andrey, Jia Xin, Assa-Munt Nuria
Abstract excerpt
Relaxation values reflecting residue-specific line broadening revealed amino acids in the DNA-binding domain of PU.1 on a surface potentially involved in protein-protein interactions. Mutation of these amino acids did not cause protein unfolding but destabilized PU.1-DNA binding. Addition of IFN response factor 4 to form the ternary complex recovered binding stability. Fluorescence quenching experiments proved...
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