MHC class I assembly: out and about
نویسندگان
چکیده
منابع مشابه
MHC class I multimers
T lymphocytes play a key role in the immune response to both foreign and self peptide antigens, which they recognize in combination with MHC molecules. In the past it has been difficult to analyse objectively the specificity, frequency and intensity of T cell responses. The recent application of fluorescent-labelled MHC class I multimers, however, has provided a powerful experimental approach t...
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Few studies have been conducted on the causative factors associated with the development of cancer. Infection by high risk human papillomaviruses (HPVs) have been implicated as causative agents in a variety of cancers. HPV is capable of evading immune system and establishing persistent infections. Prolonged infection and lesion maintenance are associated with higher risk of neoplastic progressi...
متن کاملInteraction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum.
The endoplasmic reticulum (ER) protein Bap31 associates with nascent class I MHC molecules. It appears to mediate the export of class I MHC molecules from the ER and may also be involved in their quality control. In this study, we use Förster resonance energy transfer and quantitative fluorescence imaging to show that in human, HeLa cells, Bap31 clusters with MHC class I (HLA-A2) molecules in t...
متن کاملMHC class I molecules, structure and function.
MHC class I molecules (MHC-I) are cell surface recognition elements expressed on virtually all somatic cells. These molecules sample peptides generated within the cell and signal the cell's physiological state to effector cells of the immune system, both T lymphocytes and natural killer (NK) cells. In addition, molecules structurally related to MHC-I, collectively known as MHC-Ib, are more spec...
متن کاملComplex assembly, crystallization and preliminary X-ray crystallographic studies of duck MHC class I molecule.
In order to understand the biological properties of the immune systems of waterfowl and to establish a system for structural studies of duck class I major histocompatibility complex (DuMHC I), a complex of DuMHC I with duck beta(2)-microglobulin (Dubeta(2)m) and the peptide AEIEDLIF (AF8) derived from H5N1 NP residues 251-258 was assembled. The complex was crystallized; the crystals belonged to...
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ژورنال
عنوان ژورنال: Trends in Immunology
سال: 2008
ISSN: 1471-4906
DOI: 10.1016/j.it.2008.06.004