In this section
@article{Voisin:2023:10.3390/toxins15070430,
author = {Voisin, TB and Couves, EC and Tate, EW and Bubeck, D},
doi = {10.3390/toxins15070430},
journal = {Toxins},
title = {Dynamics and molecular interactions of GPI-anchored CD59},
url = {http://dx.doi.org/10.3390/toxins15070430},
volume = {15},
year = {2023}
}
TY - JOUR
AB - CD59 is a GPI-anchored cell surface receptor that serves as a gatekeeper to controlling pore formation. It is the only membrane-bound inhibitor of the complement membrane attack complex (MAC), an immune pore that can damage human cells. While CD59 blocks MAC pores, the receptor is co-opted by bacterial pore-forming proteins to target human cells. Recent structures of CD59 in complexes with binding partners showed dramatic differences in the orientation of its ectodomain relative to the membrane. Here, we show how GPI-anchored CD59 can satisfy this diversity in binding modes. We present a PyLipID analysis of coarse-grain molecular dynamics simulations of a CD59-inhibited MAC to reveal residues of complement proteins (C6:Y285, C6:R407 C6:K412, C7:F224, C8β:F202, C8β:K326) that likely interact with lipids. Using modules of the MDAnalysis package to investigate atomistic simulations of GPI-anchored CD59, we discover properties of CD59 that encode the flexibility necessary to bind both complement proteins and bacterial virulence factors.
AU - Voisin,TB
AU - Couves,EC
AU - Tate,EW
AU - Bubeck,D
DO - 10.3390/toxins15070430
PY - 2023///
SN - 2072-6651
TI - Dynamics and molecular interactions of GPI-anchored CD59
T2 - Toxins
UR - http://dx.doi.org/10.3390/toxins15070430
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:001036345400001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=a2bf6146997ec60c407a63945d4e92bb
UR - https://www.mdpi.com/2072-6651/15/7/430
VL - 15
ER -
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