IMPORTANCE OF PEPTIDE AMINO AND CARBOXYL TERMINI TO THE STABILITY OF MHC CLASS-I MOLECULES
IMPORTANCE OF PEPTIDE AMINO AND CARBOXYL TERMINI TO THE STABILITY OF MHC CLASS-I MOLECULES
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DOI：
10.1126/science.8023162
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发表时间：
1994-07-15
期刊：
影响因子：
56.9
通讯作者：
WILEY, DC
中科院分区：
文献类型：
--
作者：
BOUVIER, M;WILEY, DC
一种流感病毒基质肽，其中带电荷的氨基或羧基末端被甲基取代，促进了 I 类人组织相容性抗原 (HLA-A2) 的折叠。在两个末端修饰的肽不会促进稳定折叠。与不具有任一末端的肽复合的 HLA-A2 的热稳定性与对照肽相比低 22°C，而两个锚定位置都被丙氨酸取代的基质肽的稳定性仅降低了 5.5°C。因此，肽结合位点两端的保守的主要组织相容性复合物 I 类残基形成了对于热稳定性至关重要的位点。 结合短肽的末端。
An influenza virus matrix peptide in which either the charged amino or carboxyl terminus was substituted by methyl groups promoted folding of the class I human histocompatibility antigen (HLA-A2). A peptide modified at both termini did not promote stable folding. The thermal stability of HLA-A2 complexed with peptides that did not have either terminus was similar to 22 degrees C lower than that of the control peptide, whereas matrix peptide in which both anchor positions were substituted by alanines had its stability decreased by only 5.5 degrees C. Thus, the conserved major histocompatibility complex class I residues at both ends of the peptide binding site form energetically important sites for binding the termini of short peptides.