2LPF

R state structure of monomeric phospholamban (C36A, C41F, C46A)

2LPF の概要

• エントリーDOI: 10.2210/pdb2lpf/pdb
• 関連するPDBエントリー: 1N7L 2KB7 2KYV
• NMR情報: BMRB: 18256
• 分子名称: Cardiac phospholamban (1 entity in total)
• 機能のキーワード: phospholamban, membrane protein, excited state, dilated cardiomyopathy
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Sarcoplasmic reticulum membrane; Single-pass membrane protein (By similarity): P61015
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6150.48

構造登録者

De Simone, A.,Montalvao, R.W.,Gustavsson, M.,Shi, L.,Veglia, G.,Vendruscolo, M. (登録日: 2012-02-11, 公開日: 2013-02-13, 最終更新日: 2024-05-15)

主引用文献

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

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: 23968132
DOI: 10.1021/bi400517b

実験手法

SOLUTION NMR