Interdomain Fluorescence Resonance Energy Transfer in SERCA Probed by Cyan-Fluorescent Protein Fused to the Actuator Domain
Author:
Affiliation:
1. Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi702089j
Reference70 articles.
1. Interaction of Nucleotides with Asp351 and the Conserved Phosphorylation Loop of Sarcoplasmic Reticulum Ca2+-ATPase
2. Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPase
3. Functional consequences of alterations to amino acids located in the nucleotide binding domain of the Ca2(+)-ATPase of sarcoplasmic reticulum.
4. Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells.
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