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Superinhibitory Phospholamban Mutants Compete with Ca(2+) for Binding to SERCA2a by Stabilizing a Unique Nucleotide-dependent Conformational State

Three cross-linkable phospholamban (PLB) mutants of increasing inhibitory strength (N30C-PLB < N27A,N30C,L37A-PLB (PLB3) < N27A,N30C,L37A,V49G-PLB (PLB4)) were used to determine whether PLB decreases the Ca(2+) affinity of SERCA2a by competing for Ca(2+) binding. The functional effects of N30C...

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Autori principali: Akin, Brandy L., Chen, Zhenhui, Jones, Larry R.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Biochemistry and Molecular Biology 2010
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2937880/
https://ncbi.nlm.nih.gov/pubmed/20622261
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.151779
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