Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation
Polley, Anirban; Orłowski, Adam; Danne, Reinis; Gurtovenko, Andrey A.; Bernardino de La Serna, Jorge; Eggeling, Christian; Davis, Simon J.; Róg, Tomasz; Vattulainen, Ilpo (2017-03-02)
Polley, Anirban
Orłowski, Adam
Danne, Reinis
Gurtovenko, Andrey A.
Bernardino de La Serna, Jorge
Eggeling, Christian
Davis, Simon J.
Róg, Tomasz
Vattulainen, Ilpo
02.03.2017
Julkaisun pysyvä osoite on
https://urn.fi/URN:NBN:fi:tty-201801231120
https://urn.fi/URN:NBN:fi:tty-201801231120
Kuvaus
Peer reviewed
Tiivistelmä
Proteins embedded in the plasma membrane mediate interactions with the cell environment and play decisive roles in many signaling events. For cell-cell recognition molecules, it is highly likely that their structures and behavior have been optimized in ways that overcome the limitations of membrane tethering. In particular, the ligand binding regions of these proteins likely need to be maximally exposed. Here we show by means of atomistic simulations of membrane-bound CD2, a small cell adhesion receptor expressed by human T-cells and natural killer cells, that the presentation of its ectodomain is highly dependent on membrane lipids and receptor glycosylation acting in apparent unison. Detailed analysis shows that the underlying mechanism is based on electrostatic interactions complemented by steric interactions between glycans in the protein and the membrane surface. The findings are significant for understanding the factors that render membrane receptors accessible for binding and signaling.
Kokoelmat
- TUNICRIS-julkaisut [16740]