Stability of empty and peptide-loaded class II major histocompatibility complex molecules at neutral and endosomal pH: comparison to class I proteins.
The structure and thermal stability of empty and peptide-filled forms of the murine class II major histocompatibility complex (MHC) molecule I-E(k) were studied at neutral and mildly acidic pH. The two forms have distinct circular dichroic spectra, suggesting that a conformational change may accompa...
المؤلفون الرئيسيون: | Reich, Z, Altman, J, Boniface, J, Lyons, D, Kozono, H, Ogg, G, Morgan, C, Davis, M |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1997
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مواد مشابهة
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Insight into the structure and function of empty class II major histocompatibility complexes
حسب: Carven, Gregory J. (Gregory John), 1975-
منشور في: (2005) -
The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules.
حسب: Cerundolo, V, وآخرون
منشور في: (1991) -
Empty MHC class I molecules come out in the cold.
حسب: Ljunggren, H, وآخرون
منشور في: (1990) -
EMPTY MHC CLASS-I MOLECULES COME OUT IN THE COLD
حسب: Ljunggren, H, وآخرون
منشور في: (1990) -
Defective assembly of class I major histocompatibility complex molecules in an embryonic cell line.
حسب: Bikoff, E, وآخرون
منشور في: (1991)