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...
Päätekijät: | Reich, Z, Altman, J, Boniface, J, Lyons, D, Kozono, H, Ogg, G, Morgan, C, Davis, M |
---|---|
Aineistotyyppi: | Journal article |
Kieli: | English |
Julkaistu: |
1997
|
Samankaltaisia teoksia
-
The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules.
Tekijä: Cerundolo, V, et al.
Julkaistu: (1991) -
Insight into the structure and function of empty class II major histocompatibility complexes
Tekijä: Carven, Gregory J. (Gregory John), 1975-
Julkaistu: (2005) -
Modulation of the major histocompatibility complex class II-associated peptide repertoire by human histocompatibility leukocyte antigen (HLA)-DO.
Tekijä: van Ham, M, et al.
Julkaistu: (2000) -
Association of class I major histocompatibility heavy and light chains induced by viral peptides.
Tekijä: Townsend, A, et al.
Julkaistu: (1989) -
Empty MHC class I molecules come out in the cold.
Tekijä: Ljunggren, H, et al.
Julkaistu: (1990)