Campbell K S, Bäckström B T, Tiefenthaler G, Palmer E
The Basel Institute for Immunology, Switzerland.
Semin Immunol. 1994 Dec;6(6):393-410. doi: 10.1006/smim.1994.1049.
We have compared the transmembrane sequences of 72 vertebrate antigen receptor (mIg and TCR) polypeptides. This allowed us to identify a Conserved Antigen Receptor Transmembrane (CART) motif which is present in all antigen receptor transmembrane domains from species as far removed as cartilaginous fish. Most of the amino acids in the CART motif are polar or aromatic and may interact with other proteins in the lipid environment. In addition, modeling the antigen receptor transmembrane domain in an alpha helical conformation places the CART residues on one face of the alpha helix. Thus, the CART motif may encode a structural unit which plays a role in the assembly and/or the signaling properties of lymphocyte antigen receptors. We speculate on the potential role of the CART motifs in lymphocyte signaling.
我们比较了72种脊椎动物抗原受体（mIg和TCR）多肽的跨膜序列。这使我们能够识别出一种保守的抗原受体跨膜（CART）基序，该基序存在于从软骨鱼到远亲物种的所有抗原受体跨膜结构域中。CART基序中的大多数氨基酸是极性或芳香性的，可能在脂质环境中与其他蛋白质相互作用。此外，将抗原受体跨膜结构域建模为α螺旋构象会使CART残基位于α螺旋的一侧。因此，CART基序可能编码一个在淋巴细胞抗原受体的组装和/或信号传导特性中起作用的结构单元。我们推测了CART基序在淋巴细胞信号传导中的潜在作用。
