In this section
@article{Hohenester:2015:10.1016/j.str.2015.09.004,
author = {Hohenester, E and Paracuellos, P and Briggs, DC and Carafoli, F and Loncar, T},
doi = {10.1016/j.str.2015.09.004},
journal = {Structure},
pages = {2133--2142},
title = {Insights into collagen uptake by C-type mannose receptors from the crystal structure of Endo180 domains 1-4},
url = {http://dx.doi.org/10.1016/j.str.2015.09.004},
volume = {23},
year = {2015}
}
TY - JOUR
AB - The C-type mannose receptor and its homologEndo180 (or uPARAP, for urokinase plasminogenactivator receptor-associated protein) mediate theendocytic uptake of collagen by macrophages and fi-broblasts. This process is required for normal tissueremodeling, but also facilitates the growth anddissemination of tumors. We have determined thecrystal structure at 2.5 A resolution of the N-terminalregion of Endo180, consisting of a ricin-like domain,a fibronectin type II (FN2) domain, and two C-typelectin (CTL) domains. The L-shaped arrangement ofthese domains creates a shallow trench spanningthe FN2 and CTL1 domains, which was shown bymutagenesis to bind triple-helical and denaturedcollagen. Small-angle X-ray scattering showed thatthe L-shaped structure is maintained in solution atneutral and acidic pH, irrespective of calcium ionloading. Collagen binding was equally unaffectedby acidic pH, suggesting that collagen release in endosomesis not regulated by changes within theEndo180 N-terminal region.
AU - Hohenester,E
AU - Paracuellos,P
AU - Briggs,DC
AU - Carafoli,F
AU - Loncar,T
DO - 10.1016/j.str.2015.09.004
EP - 2142
PY - 2015///
SN - 1878-4186
SP - 2133
TI - Insights into collagen uptake by C-type mannose receptors from the crystal structure of Endo180 domains 1-4
T2 - Structure
UR - http://dx.doi.org/10.1016/j.str.2015.09.004
UR - http://hdl.handle.net/10044/1/26859
VL - 23
ER -
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