Anchoring mechanisms of membrane-associated M13 major coat protein
Anchoring mechanisms of membrane-associated M13 major coat protein
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DOI：
10.1016/j.chemphyslip.2006.02.023
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发表时间：
2006-06-01
影响因子：
3.4
通讯作者：
Hemminga, Marcus A.
中科院分区：
文献类型：
--
作者：
Stopar, David;Spruijt, Ruud B.;Hemminga, Marcus A.
噬菌体M13主要外壳蛋白被广泛用作研究膜蛋白的生物物理、生物化学和分子生物学参考系统。蛋白质有几个元素，控制其在脂质双层中的位置和方向。N-末端主要由带负电荷的氨基酸残基（Glu 2、Asp 4和Asp 5）的存在所支配，这些氨基酸残基总是试图延伸到水相中，因此充当亲水性锚。两亲和疏水跨膜部分包含最重要的疏水锚定元件。此外，在这些结构域（Phe 11、Tyr 21、Tyr 24、Trp 26、Phe 42、Phe 45、Lys 40、Lys 43和Lys 44）中存在特定的芳香族和带电荷的氨基酸残基，这些残基微调蛋白质与脂质双层的缔合。界面Tyr残基是蛋白质精确定位的重要识别元件。具有脂肪族特征的残基不能最佳地执行的功能。Trp 26锚不是很强：取决于上下文，色氨酸残基可以移入或移出膜。另一方面，在蛋白质C-末端的Lys残基和Phe残基以独特的协同作用起作用，以将蛋白质牢固地锚在脂质双层中。(c)2006爱思唯尔爱尔兰有限公司保留所有权利。
Bacteriophage M13 major coat protein is extensively used as a biophysical, biochemical, and molecular biology reference system for studying membrane proteins. The protein has several elements that control its position and orientation in a lipid bilayer. The N-terminus is dominated by the presence of negatively charged amino acid residues (Glu2, Asp4, and Asp5), which will always try to extend into the aqueous phase and therefore act as a hydrophilic anchor. The amphipathic and the hydrophobic transmembrane part contain the most important hydrophobic anchoring elements. In addition there are specific aromatic and charged amino acid residues in these domains (Phe11, Tyr21, Tyr24, Trp26, Phe42, Phe45, Lys40, Lys43, and Lys44) that fine-tune the association of the protein to the lipid bilayer. The interfacial Tyr residues are important recognition elements for precise protein positioning. a function that cannot be performed optimally by residues with an aliphatic character. The Trp26 anchor is not very strong: depending on the context, the tryptophan residue may move in or out of the membrane. On the other hand, Lys residues and Phe residues at the C-terminus of the protein act in a unique concerted action to strongly anchor the protein in the lipid bilayer. (c) 2006 Elsevier Ireland Ltd. All rights reserved.