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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes
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Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes

机译：Na +，K + -ATP酶与膜的N-末端肽类似物的相互作用

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摘要

The Na+,K+-ATPase, which is present in the plasma membrane of all animal cells, plays a crucial role in maintaining the Na+ and K+ electrochemical potential gradients across the membrane. Recent studies have suggested that the N-terminus of the protein's catalytic alpha-subunit is involved in an electrostatic interaction with the surrounding membrane, which controls the protein's conformational equilibrium. However, because the N-terminus could not yet be resolved in any X-ray crystal structures, little information about this interaction is so far available. In measurements utilising poly-L-lysine as a model of the protein's lysine-rich N-terminus and using lipid vesicles of defined composition, here we have identified the most likely origin of the interaction as one between positively charged lysine residues of the N-terminus and negatively charged headgroups of phospholipids (notably phosphatidylserine) in the surrounding membrane. Furthermore, to isolate which segments of the N-terminus could be involved in membrane binding, we chemically synthesized N-terminal fragments of various lengths. Based on a combination of results from RH421 UV/visible absorbance measurements and solid-state P-31 and H-2 NMR using these N-terminal fragments as well as MD simulations it appears that the membrane interaction arises from lysine residues prior to the conserved LKKE motif of the N-terminus. The MD simulations indicate that the strength of the interaction varies significantly between different enzyme conformations.
机译：存在于所有动物细胞的血浆膜中的Na +，K + -ATP酶在将Na +和K +电化学潜在梯度穿过膜上起着至关重要的作用。最近的研究表明，蛋白质催化α-亚基的N-末端参与与周围膜的静电相互作用，其控制蛋白质的构象平衡。但是，因为在任何X射线晶体结构中尚未解决N-Terminus，所以迄今为止关于该交互的信息很少。在测量利用聚-L-赖氨酸作为富含蛋白质的富含N-末端的模型以及使用定义组合物的脂质囊泡，在这里，我们已经将最可能的相互作用起源鉴定为N-带正电荷的赖氨酸残基之间的相互作用的起源在周围膜中磷脂（特别是磷脂酰丝氨酸）的末端和带负电荷的头组。此外，分离N-末端的哪个区段可以参与膜结合，我们化学合成各种长度的N-末端片段。基于RH421 UV /可见光率测量和使用这些N-末端片段的固态P-31和H-2 NMR的结果的组合，以及MD模拟，看起来膜相互作用在保守前从赖氨酸残基产生N-Terminus的LKKE主题。 MD模拟表明相互作用的强度在不同酶构象之间显着变化。

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