SUBSTRATE-SPECIFICITY OF ALLELIC VARIANTS OF THE TAP PEPTIDE TRANSPORTER
SUBSTRATE-SPECIFICITY OF ALLELIC VARIANTS OF THE TAP PEPTIDE TRANSPORTER
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DOI：
10.1016/s1074-7613(94)80019-7
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发表时间：
1994-12-01
期刊：
影响因子：
32.4
通讯作者：
PLOEGH, HL
中科院分区：
文献类型：
--
作者：
HEEMELS, MT;PLOEGH, HL
与抗原加工相关的转运蛋白（TAP）将肽从胞质溶胶转运到内质网（ER）腔中。易位特异性的一个重要决定因素是肽底物的C-末端残基的身份。在大鼠中，合适的C末端是必需的，但并不总是足以使肽被选择用于易位。在这里，我们表明最佳长度（9个残基）的肽内的序列限制可能会干扰转运;转运蛋白选择性地易位16聚体肽的较短衍生物，而不是16聚体本身;并且转运蛋白cim（B）等位基因在其耐受的C末端中最具选择性，在肽长度偏好方面比cim（a）变体更宽松。
The transporter associated with antigen processing (TAP) translocates peptides from the cytosol into the lumen of the endoplasmic reticulum (ER). An important determinant for the specificity of translocation is the identity of the C-terminal residue of the peptide substrate. In the rat, a suitable C terminus is necessary but not always sufficient for a peptide to be selected for translocation. Here we show that sequence constraints within a peptide of optimal length (9 residues) may interfere with transport; that the transporter selectively translocates shorter derivatives of a 16-mer peptide rather than the 16-mer itself; and that the transporter cim(b) allele, which is most selective in the C termini it will tolerate, is more relaxed in peptide length preference than is the cim(a) variant.