Identification of a PU.1-IRF4 Protein Interaction Surface Predicted by Chemical Exchange Line Broadening

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 res...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-01, Vol.100 (2), p.511-516
Hauptverfasser:	McKercher, Scott R., Lombardo, Christian R., Bobkov, Andrey, Jia, Xin, Assa-Munt, Nuria
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Binding Sites Biological Sciences Biophysics DNA DNA - metabolism DNA probes DNA-Binding Proteins - chemistry Fluorescence Genetic mutation Interferon Regulatory Factors Mutant proteins Mutation Pests Protein Conformation Proteins Proto-Oncogene Proteins - chemistry Ratios Trans-Activators - chemistry Transcription factors Transcription Factors - chemistry
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