| Автор | Fischer Lindahl, Kirsten |
| Автор | Byers, Derek E. |
| Автор | Dabhi, Vikram M. |
| Автор | Hovik, Rolf |
| Автор | Jones, Elsy P. |
| Автор | Smith, Geoffrey P. |
| Автор | Wang, Chyung-Ru |
| Автор | Xiao, Hong |
| Автор | Yoshino, Masayasu |
| Дата выпуска | 1997 |
| dc.description | ▪ Abstract H2-M3 is an MHC class Ib molecule of the mouse with a unique preference for N-formylated peptides, which may come from the N-termini of endogenous, mitochondrial proteins or foreign, bacterial proteins. The crystal structure of M3 revealed a hydrophobic peptide-binding groove with an occluded A pocket and the peptide shifted one residue relative to class Ia structures. The formyl group is held by a novel hydrogen bonding network, involving His9 on the bottom of the groove, and the side chain of the P1 methionine is lodged in the B pocket. M3 is a full-service histocompatibility (H) antigen, i.e. self-M3 can present endogenous peptides as minor H antigens and foreign, bacterial antigens in a defensive immune response to infection; and foreign M3 complexed with endogenous self-peptides can be recognized as an alloantigen. The hydrophobic groove of M3 may also allow it to present nonpeptide ligands in the manner of human CD1. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | H2-M3, A FULL-SERVICE CLASS Ib HISTOCOMPATIBILITY ANTIGEN <sup>1</sup> |
| DOI | 10.1146/annurev.immunol.15.1.851 |
| Print ISSN | 0732-0582 |
| Журнал | Annual Review of Immunology |
| Том | 15 |
| Первая страница | 851 |
| Последняя страница | 879 |
| Аффилиация | Fischer Lindahl, Kirsten; Howard Hughes Medical Institute, Departments of Microbiology and Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9050; e-mail: jharvey@howie.swmed.edu |
