Synthetic peptides mimic the assembly of transmembrane glycoproteins.
Synthetic peptides mimic the assembly of transmembrane glycoproteins.
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发表时间：
1989-03
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通讯作者：
B. Bormann;W. Knowles;V. Marchesi
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作者：
B. Bormann;W. Knowles;V. Marchesi
许多受体的膜内结构域的组成是非常均匀的，然而有证据表明，许多跨膜蛋白结合在一起，在膜内形成特异性的非共价同质复合物或异质复合物。我们合成了糖蛋白A、糖蛋白C和白细胞介素2受体Tac抗原跨膜结构域对应的肽，在体外研究了跨膜结构域之间的相互作用。合成的跨膜糖蛋白A肽与红细胞和K562细胞膜的天然糖蛋白和糖蛋白形成复合物，该复合物具有可逆性、特异性，并且可以在没有洗涤剂的天然双层系统中证明。合成的糖蛋白C和白细胞介素2受体Tac抗原跨膜肽虽然氨基酸组成相似，但不与糖蛋白相互作用，也不抑制合成的糖蛋白A跨膜肽与天然糖蛋白的结合。有人提出，受体蛋白的跨膜片段不仅包含插入和锚定所需的结构信息，还包含介导跨膜糖蛋白相互作用的特定结合位点。
The composition of the intramembranous domains of many receptors are remarkably uniform, yet there is evidence that many transmembrane proteins associate together to form specific noncovalent homo- or heterocomplexes within the membrane. We have synthesized peptides corresponding to transmembrane domains of glycophorin A, glycophorin C, and the interleukin 2-receptor Tac antigen to study the interactions between transmembrane domains in vitro. Synthetic transmembrane glycophorin A peptide formed a complex with native glycophorin and glycoproteins of erythrocyte and K562 cell membranes that was reversible, specific, and could be demonstrated in a natural bilayer system in the absence of detergents. Synthetic glycophorin C and interleukin 2-receptor Tac antigen transmembrane peptides, although similar in amino acid composition, did not interact with glycophorin and did not inhibit the binding of the synthetic glycophorin A transmembrane peptide to native glycophorin. It is proposed that the transmembrane segments of receptor proteins contain not only the structural information necessary for insertion and anchoring but specific binding sites that mediate interactions between transmembrane glycoproteins.