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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Biochemistry and Molecular Biology
2010
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| Témata: | |
| On-line přístup: | 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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