Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 24, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/ijms24010011
Keywords
Ly6 proteins; Ly6; uPAR; three-finger proteins; GPI-anchored proteins; N-glycans; O-glycans; molecular dynamics; orientational analysis; protein-membrane interactions
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Ly6/uPAR proteins with GPI-anchors have various positions and orientations on the membrane surface, regardless of the linker length between the LU domain and GPI-anchor. The proteins interact with the membrane through polypeptide parts and glycans. Different proteins have different contact regions with the membrane and unique orientations, indicating that GPI-anchoring does not determine the optimal pre-orientation for receptor interaction.
Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single beta-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide parts and N-/O-glycans. Lynx1, Lynx2, Lypd6B, and Ly6H contacted the membrane by the loop regions responsible for interactions with nicotinic acetylcholine receptors, while Lypd6 and CD59 demonstrated unique orientations with accessible receptor-binding sites. Thus, GPI-anchoring does not guarantee an optimal 'pre-orientation' of the LU domain for the receptor interaction.
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