Bouvier M, Wiley D C
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
Science. 1994 Jul 15;265(5170):398-402. doi: 10.1126/science.8023162.
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 approximately 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.
一种流感病毒基质肽，其带电荷的氨基或羧基末端被甲基取代，促进了I类人类组织相容性抗原（HLA - A2）的折叠。两端都被修饰的肽不能促进稳定折叠。与没有任何一端修饰的肽复合的HLA - A2的热稳定性比对照肽低约22摄氏度，而两个锚定位点都被丙氨酸取代的基质肽其稳定性仅降低了5.5摄氏度。因此，肽结合位点两端保守的主要组织相容性复合体I类残基形成了与短肽末端结合的能量重要位点。
