Abstract
Background: TAP proteins tagged with CFP and YFP were used for FRET spectroscopy measurements. Results: Conformational changes of the nucleotide binding domains (NBD) were measurable in permeabilized cells. Conclusion: TAP-specific peptides induce NBD closure, and maximal NBD closure is induced by the combination of a peptide and a non-hydrolysable ATP analog. Significance: These studies elucidate distinct steps of the TAP transport cycle. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Geng, J., Sivaramakrishnan, S., & Raghavan, M. (2013). Analyses of conformational states of the transporter associated with antigen processing (TAP) protein in a native cellular membrane environment. Journal of Biological Chemistry, 288(52), 37039–37047. https://doi.org/10.1074/jbc.M113.504696
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