Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation

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http://hdl.handle.net/10138/224434

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Polley , A , Orlowski , A , Danne , R , Gurtovenko , A A , de la Serna , J B , Eggeling , C , Davis , S J , Rog , T & Vattulainen , I 2017 , ' Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation ' , Journal of Physical Chemistry Letters , vol. 8 , no. 5 , pp. 1060-1066 . https://doi.org/10.1021/acs.jpclett.6b02824

Titel: Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation
Författare: Polley, Anirban; Orlowski, Adam; Danne, Reinis; Gurtovenko, Andrey A.; de la Serna, Jorge Bernardino; Eggeling, Christian; Davis, Simon J.; Rog, Tomasz; Vattulainen, Ilpo
Upphovmannens organisation: Department of Physics
Datum: 2017-03-02
Språk: eng
Sidantal: 7
Tillhör serie: Journal of Physical Chemistry Letters
ISSN: 1948-7185
DOI: https://doi.org/10.1021/acs.jpclett.6b02824
Permanenta länken (URI): http://hdl.handle.net/10138/224434
Abstrakt: 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.
Subject: ADHESION MOLECULE CD2
CELL-ADHESION
CRYSTAL-STRUCTURE
T-CELLS
CHOLESTEROL
DYNAMICS
RECEPTOR
SIMULATION
MEMBRANES
CONFORMATION
116 Chemical sciences
114 Physical sciences
1182 Biochemistry, cell and molecular biology
Referentgranskad: Ja
Licens: cc_by
Användningsbegränsning: openAccess
Parallelpublicerad version: publishedVersion


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