A TYROSINE-CONTAINING MOTIF MEDIATES ER RETENTION OF CD3-EPSILON AND ADOPTS A HELIX-TURN STRUCTURE
A TYROSINE-CONTAINING MOTIF MEDIATES ER RETENTION OF CD3-EPSILON AND ADOPTS A HELIX-TURN STRUCTURE
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DOI：
10.1002/j.1460-2075.1995.tb07220.x
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发表时间：
1995-05-15
期刊：
影响因子：
11.4
通讯作者：
ALARCON, B
中科院分区：
文献类型：
--
作者：
MALLABIABARRENA, A;JIMENEZ, MA;ALARCON, B
已经通过诱变和NMR光谱表征了CD 3-κ内质网（ER）保留基序。Tyr 177、Leu 180和Arg 183参与ER滞留。基序形成伸长的α-螺旋，其中酪氨酸和亮氨酸残基紧密并置，随后是将Arg 183置于Leu 180附近的β I'转弯。由Tyr 177和+3位亮氨酸形成的结构使人联想到含酪氨酸的内吞信号所采用的β-转角结构。此外，由CD 3-CD 4基序的转铁蛋白受体（TfR）内化序列的取代仍然允许TfR的快速内化，相反，由低密度脂蛋白受体的内吞信号的CD 3-CD 4基序的取代产生的嵌合蛋白质位于ER。这些数据支持这两种类型的信号之间的功能同源性的想法。
The CD3-epsilon endoplasmic reticulum (ER) retention motif has been characterized by mutagenesis and NMR spectroscopy. Tyr177, Leu180 and Arg183 are involved in ER retention, The motif forms an elongated alpha-helix in which the tyrosine and leucine residues are closely apposed, followed by a beta I' turn that places Arg183 in the vicinity of Leu180. The structure formed by Tyr177 and the leucine in position +3 is reminiscent of the beta-turn structure adopted by tyrosine-containing endocytosis signals. Moreover, substitution of the transferrin receptor (TfR) internalization sequence by the CD3-epsilon motif still allowed the rapid internalization of the TfR and, conversely, the chimeric protein resulting from the substitution of the CD3-epsilon motif by the endocytosis signal of the low density lipoprotein receptor was ER located. These data support the idea of a functional homology between the two types of signal.