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基于酪氨酸的内吞信号识别的结构解释。

A structural explanation for the recognition of tyrosine-based endocytotic signals.

作者信息

Owen D J, Evans P R

机构信息

Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.

出版信息

Science. 1998 Nov 13;282(5392):1327-32. doi: 10.1126/science.282.5392.1327.

DOI:10.1126/science.282.5392.1327
PMID:9812899
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5600252/
Abstract

Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors.

摘要

许多细胞表面蛋白通过一个胞质序列基序（酪氨酸-X-X-（疏水残基））被标记用于内吞作用，该基序可被AP2衔接蛋白的μ2亚基识别。已在2.7埃分辨率下确定了与表皮生长因子受体和反式高尔基体网络蛋白TGN38的内化信号肽复合的μ2内化信号结合结构域的晶体结构。信号肽呈伸展构象，而非预期的紧密转角构象。特异性由结合肽中酪氨酸和亮氨酸的疏水口袋赋予。在晶体中，该蛋白形成二聚体，这可能会增强与二聚体受体结合的强度和特异性。

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2
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