2LPF
R state structure of monomeric phospholamban (C36A, C41F, C46A)
Summary for 2LPF
| Entry DOI | 10.2210/pdb2lpf/pdb |
| Related | 1N7L 2KB7 2KYV |
| NMR Information | BMRB: 18256 |
| Descriptor | Cardiac phospholamban (1 entity in total) |
| Functional Keywords | phospholamban, membrane protein, excited state, dilated cardiomyopathy |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Sarcoplasmic reticulum membrane; Single-pass membrane protein (By similarity): P61015 |
| Total number of polymer chains | 1 |
| Total formula weight | 6150.48 |
| Authors | De Simone, A.,Montalvao, R.W.,Gustavsson, M.,Shi, L.,Veglia, G.,Vendruscolo, M. (deposition date: 2012-02-11, release date: 2013-02-13, Last modification date: 2024-05-15) |
| Primary citation | De Simone, A.,Gustavsson, M.,Montalvao, R.W.,Shi, L.,Veglia, G.,Vendruscolo, M. Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation. Biochemistry, 52:6684-6694, 2013 Cited by PubMed Abstract: Phospholamban is an integral membrane protein that controls the calcium balance in cardiac muscle cells. As the function and regulation of this protein require the active involvement of low populated states in equilibrium with the native state, it is of great interest to acquire structural information about them. In this work, we calculate the conformations and populations of the ground state and the three main excited states of phospholamban by incorporating nuclear magnetic resonance residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations. We then provide a description of the manner in which phosphorylation at Ser16 modulates the activity of the protein by increasing the sizes of the populations of its excited states. These results demonstrate that the approach that we describe provides a detailed characterization of the different states of phospholamban that determine the function and regulation of this membrane protein. We anticipate that the knowledge of conformational ensembles enable the design of new dominant negative mutants of phospholamban by modulating the relative populations of its conformational substates. PubMed: 23968132DOI: 10.1021/bi400517b PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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