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• W2896047662 endingPage "31" @default.
• W2896047662 startingPage "15" @default.
• W2896047662 abstract "Classical HLA class II molecules are highly polymorphic heterodimeric transmembrane proteins encoded by a polygenic cluster on chromosome 6. Polymorphic residues in the membrane-distal domains ensure that a large collection of microbial peptides can be bound in the human population. Still, the HLA-DR, -DP and -DQ isotypes show a high degree of conservation in their overall tertiary and quaternary structures, in line with their common function in T cell receptor activation. Interestingly, the primary structure of the intracellular domains are highly divergent between isotypes and they also show allotypic variations. The functional impact of these differences remains to be fully appreciated. Here, we address the role of the MHC class II cytoplasmic tails in intracellular trafficking. First, the emphasis will be on the interplay between the cytoplasmic domains of classical human MHC class II molecules and those of the invariant chain chaperone (CD74) isoforms. Then, we will examine the importance of the highly conserved β-chain cytoplasmic lysine residue in the ubiquitin-driven trafficking of MHC class II molecules. These considerations should help understand the potential functional impact of sequence variations that may arise in the cytoplasmic tails and transmembrane domains of MHC class II molecules." @default.
• W2896047662 created "2018-10-26" @default.
• W2896047662 creator A5030684999 @default.
• W2896047662 creator A5039697077 @default.
• W2896047662 creator A5050286646 @default.
• W2896047662 date "2019-01-01" @default.
• W2896047662 modified "2023-10-01" @default.
• W2896047662 title "On the structure–function of MHC class II molecules and how single amino acid polymorphisms could alter intracellular trafficking" @default.
• W2896047662 cites W113162970 @default.
• W2896047662 cites W130273196 @default.
• W2896047662 cites W1483922594 @default.
• W2896047662 cites W1494319977 @default.
• W2896047662 cites W1495214173 @default.
• W2896047662 cites W1507598785 @default.
• W2896047662 cites W1518401857 @default.
• W2896047662 cites W1525290983 @default.
• W2896047662 cites W1534119722 @default.
• W2896047662 cites W1538684146 @default.
• W2896047662 cites W1553862381 @default.
• W2896047662 cites W1570667313 @default.
• W2896047662 cites W1571391036 @default.
• W2896047662 cites W15726773 @default.
• W2896047662 cites W1575311801 @default.
• W2896047662 cites W1585391064 @default.
• W2896047662 cites W1596896862 @default.
• W2896047662 cites W1610527166 @default.
• W2896047662 cites W1618328770 @default.
• W2896047662 cites W1624269400 @default.
• W2896047662 cites W1634187189 @default.
• W2896047662 cites W1637404187 @default.
• W2896047662 cites W1734730736 @default.
• W2896047662 cites W1767948410 @default.
• W2896047662 cites W1772475411 @default.
• W2896047662 cites W1874651941 @default.
• W2896047662 cites W1939938623 @default.
• W2896047662 cites W1955514812 @default.
• W2896047662 cites W1963584953 @default.
• W2896047662 cites W1963622435 @default.
• W2896047662 cites W1963809182 @default.
• W2896047662 cites W1968959087 @default.
• W2896047662 cites W1969286200 @default.
• W2896047662 cites W1970138249 @default.
• W2896047662 cites W1973459107 @default.
• W2896047662 cites W1974989648 @default.
• W2896047662 cites W1975696393 @default.
• W2896047662 cites W1975963956 @default.
• W2896047662 cites W1976703529 @default.
• W2896047662 cites W1977631515 @default.
• W2896047662 cites W1977959719 @default.
• W2896047662 cites W1979751962 @default.
• W2896047662 cites W1980202013 @default.
• W2896047662 cites W1980822710 @default.
• W2896047662 cites W1980827057 @default.
• W2896047662 cites W1982684150 @default.
• W2896047662 cites W1983122260 @default.
• W2896047662 cites W1984288819 @default.
• W2896047662 cites W1984731860 @default.
• W2896047662 cites W1986321004 @default.
• W2896047662 cites W1987275221 @default.
• W2896047662 cites W1988076285 @default.
• W2896047662 cites W1988723232 @default.
• W2896047662 cites W1989941778 @default.
• W2896047662 cites W1990091683 @default.
• W2896047662 cites W1990221491 @default.
• W2896047662 cites W1992207446 @default.
• W2896047662 cites W1992438598 @default.
• W2896047662 cites W1993655108 @default.
• W2896047662 cites W1993923133 @default.
• W2896047662 cites W1995413714 @default.
• W2896047662 cites W1995524511 @default.
• W2896047662 cites W1996291400 @default.
• W2896047662 cites W1996787456 @default.
• W2896047662 cites W1997507341 @default.
• W2896047662 cites W1998434423 @default.
• W2896047662 cites W1999410205 @default.
• W2896047662 cites W2000562739 @default.
• W2896047662 cites W2000738263 @default.
• W2896047662 cites W2001737867 @default.
• W2896047662 cites W2002377650 @default.
• W2896047662 cites W2003769309 @default.
• W2896047662 cites W2003884388 @default.
• W2896047662 cites W2004993844 @default.
• W2896047662 cites W2005263933 @default.
• W2896047662 cites W2006493141 @default.
• W2896047662 cites W2007881211 @default.
• W2896047662 cites W2008611743 @default.
• W2896047662 cites W2008933642 @default.
• W2896047662 cites W2010800833 @default.
• W2896047662 cites W2010867882 @default.
• W2896047662 cites W2010896374 @default.
• W2896047662 cites W2010946325 @default.
• W2896047662 cites W2012394593 @default.
• W2896047662 cites W2012401440 @default.
• W2896047662 cites W2012507946 @default.
• W2896047662 cites W2012952808 @default.
• W2896047662 cites W2013142337 @default.
• W2896047662 cites W2014115532 @default.
• W2896047662 cites W2015611329 @default.

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