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

Show simple item record Polley, Anirban Orlowski, Adam Danne, Reinis Gurtovenko, Andrey A. de la Serna, Jorge Bernardino Eggeling, Christian Davis, Simon J. Rog, Tomasz Vattulainen, Ilpo 2017-09-21T10:28:00Z 2017-09-21T10:28:00Z 2017-03-02
dc.identifier.citation 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 .
dc.identifier.other PURE: 82253986
dc.identifier.other PURE UUID: af86d54c-00f7-46d1-8c69-e16148274045
dc.identifier.other WOS: 000395619100027
dc.identifier.other Scopus: 85014304459
dc.identifier.other ORCID: /0000-0001-7408-3214/work/31552198
dc.description.abstract 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. en
dc.format.extent 7
dc.language.iso eng
dc.relation.ispartof Journal of Physical Chemistry Letters
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject CELL-ADHESION
dc.subject T-CELLS
dc.subject CHOLESTEROL
dc.subject DYNAMICS
dc.subject RECEPTOR
dc.subject SIMULATION
dc.subject MEMBRANES
dc.subject 116 Chemical sciences
dc.subject 114 Physical sciences
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title Glycosylation and Lipids Working in Concert Direct CD2 Ectodomain Orientation and Presentation en
dc.type Article
dc.contributor.organization Department of Physics
dc.description.reviewstatus Peer reviewed
dc.relation.issn 1948-7185
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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