Lu Linh, Vollmer Jörg, Moulon Corinne, Weltzien Hans Ulrich, Marrack Philippa, Kappler John
Howard Hughes Medical Institute, Integrated Department of Immunology, National Jewish Medical and Research Center, Denver, CO 80206, USA.
J Exp Med. 2003 Mar 3;197(5):567-74. doi: 10.1084/jem.20021762.
The major histocompatibility complex (MHC) restriction element for a human Ni(2+) reactive T cell, ANi-2.3, was identified as DR52c. A series of experiments established that the functional ligand for this T cell was a preformed complex of Ni(2+) bound to the combination of DR52c and a specific peptide that was generated in human and mouse B cells, but not in fibroblasts nor other antigen processing-deficient cells. In addition, ANi-2.3 recognition of this complex was dependent on His81 of the MHC beta chain, suggesting a role for this amino acid in Ni(2+) binding to MHC. We propose a general model for Ni(2+) recognition in which betaHis81 and two amino acids from the NH(2)-terminal part of the MHC bound peptide coordinate Ni(2+) which then interacts with some portion of the Valpha CDR1 or CDR2 region.
人类镍离子（Ni²⁺）反应性T细胞ANi - 2.3的主要组织相容性复合体（MHC）限制元件被鉴定为DR52c。一系列实验证实，该T细胞的功能性配体是一种预先形成的复合物，其中Ni²⁺与DR52c和一种特定肽结合，这种肽在人和小鼠B细胞中产生，但在成纤维细胞或其他抗原加工缺陷细胞中不产生。此外，ANi - 2.3对该复合物的识别依赖于MHCβ链的His81，表明该氨基酸在Ni²⁺与MHC结合中起作用。我们提出了一个Ni²⁺识别的通用模型，其中β链His81和来自MHC结合肽NH₂末端部分的两个氨基酸协调Ni²⁺，然后Ni²⁺与Vα CDR1或CDR2区域的某些部分相互作用。
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