The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9
The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9
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DOI：
10.1002/eji.1830270517
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发表时间：
1997-03-01
影响因子：
5.4
通讯作者：
McMichael, A
中科院分区：
文献类型：
--
作者：
Braud, V;Jones, EY;McMichael, A
人类组织相容性白细胞抗原E（HLA-E）和小鼠主要组织相容性复合体（MHC）Ib类抗原Qa-1在两个通常保守的位置143和147处共享相同的取代，这可能影响肽的C末端的结合。Qa-1能够结合源自H-2 D和H-2 L分子的前导序列的肽。我们开发了一种体外肽结合试验，以比较HLA-E与小鼠MHC Ib类分子Qa-1的结合特异性。我们证明，HLA-E结合，虽然很差，结合到Qa-1的肽，它也结合从人MHC I类分子的九聚体信号序列衍生的肽。使用丙氨酸和甘氨酸取代，我们可以在位置2和9处定义初级锚残基，并且在位置7和可能的3处定义次级锚残基。
Human histocompatibility leukocyte antigen E (HLA-E) and mouse major histocompatibility complex (MHC) class Ib antigen, Qa-1, share the same substitutions at two normally conserved positions 143 and 147, which are likely to affect binding of the C terminus of peptides. Qa-1 is able to bind a peptide derived from the leader sequence of H-2 D and H-2 L molecules. We developed a peptide binding assay in vitro to compare the binding specificity of HLA-E with the mouse MHC class Ib molecule Qa-1. We demonstrate that HLA-E binds, although poorly, the peptide which binds to Qa-1 and that it also binds nonamer signal sequence-derived peptides from human MHC class I molecules. Using alanine and glycine substitutions, we could define primary anchor residues at positions 2 and 9 and secondary anchor residues at position 7 and possibly 3.