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首页> 外文期刊>Biochemistry >Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta3 subunit by NMR spectroscopy
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Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta3 subunit by NMR spectroscopy

机译：核磁共振波谱法表征整联蛋白β3亚基的跨膜和胞质域的单体形式

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摘要

We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and cytoplasmic domains, by nuclear magnetic resonance spectroscopy. Under conditions in which it is monomeric in dodecylphosphocholine micelles, the protein consists mainly of alpha-helical structures. An amino-terminal helix corresponding to the beta3 transmembrane helix extends into the membrane-proximal region of the cytoplasmic domain. Moreover, following an apparent hinge at residues H722-D723, residues K725-A735 are mostly alpha-helical. In the presence of membrane-mimicking detergents, the cytoplasmic domain connected to the transmembrane helix is substantially ordered at pH 4.8 and 50 deg C. Its carboxyl-terminal end takes on a turn-helix configuration characteristic of the immunoreceptor tyrosine-based activation motif. These structural features of the beta3 subunit should help to explain its interaction with numerous cytosolic interacting proteins and begin to illuminate the mechanism of integrin activation.
机译：我们已经通过核磁共振波谱表征了膜蛋白，该膜蛋白包含整联蛋白β3亚基的残基P688-T762，包括其跨膜和胞质域。在十二烷基磷酸胆碱胶束中为单体的条件下，该蛋白质主要由α-螺旋结构组成。对应于β3跨膜螺旋的氨基末端螺旋延伸到细胞质结构域的膜近端区域。此外，在残基H722-D723上有明显的铰链之后，残基K725-A735主要是α-螺旋。在存在模仿膜的去污剂的情况下，连接至跨膜螺旋的胞质结构域在pH 4.8和50摄氏度时基本上是有序的。其羧基末端具有基于免疫受体酪氨酸的活化基序的特征。 beta3亚基的这些结构特征应有助于解释其与众多胞质相互作用蛋白的相互作用，并开始阐明整联蛋白激活的机制。

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