BibTex format
@article{Polley:2017:10.1021/acs.jpclett.6b02824,
author = {Polley, A and Orlowski, A and Danne, R and Gurtovenko, AA and Bernardino, de la Serna J and Eggeling, C and Davis, SJ and Rog, T and Vattulainen, I},
doi = {10.1021/acs.jpclett.6b02824},
journal = {Journal of Physical Chemistry Letters},
pages = {1060--1066},
title = {Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation},
url = {http://dx.doi.org/10.1021/acs.jpclett.6b02824},
volume = {8},
year = {2017}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - Proteins embedded in the plasma membrane mediate interactions with the cell environment and play decisiveroles in many signaling events. For cell−cell recognition molecules, it is highly likely that their structures and behavior have beenoptimized in ways that overcome the limitations of membrane tethering. In particular, the ligand binding regions of theseproteins likely need to be maximally exposed. Here we show by means of atomistic simulations of membrane-bound CD2, a smallcell adhesion receptor expressed by human T-cells and natural killer cells, that the presentation of its ectodomain is highlydependent on membrane lipids and receptor glycosylation acting in apparent unison. Detailed analysis shows that the underlyingmechanism is based on electrostatic interactions complemented by steric interactions between glycans in the protein and themembrane surface. The findings are significant for understanding the factors that render membrane receptors accessible forbinding and signaling.
AU - Polley,A
AU - Orlowski,A
AU - Danne,R
AU - Gurtovenko,AA
AU - Bernardino,de la Serna J
AU - Eggeling,C
AU - Davis,SJ
AU - Rog,T
AU - Vattulainen,I
DO - 10.1021/acs.jpclett.6b02824
EP - 1066
PY - 2017///
SN - 1948-7185
SP - 1060
TI - Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation
T2 - Journal of Physical Chemistry Letters
UR - http://dx.doi.org/10.1021/acs.jpclett.6b02824
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000395619100027&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/69264
VL - 8
ER -