Structural aspects of N-glycosylations and the C-terminal region in human glypican-1.

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title = "Structural aspects of N-glycosylations and the C-terminal region in human glypican-1.",
abstract = "Glypicans are multifunctional cell surface proteoglycans involved in several important cellular signalling pathways. Glypican-1 (Gpc1) is the predominant heparan sulphate (HS) proteoglycan in the developing and adult human brain. The two N-linked glycans and the C-terminal domain that attaches the core protein to the cell membrane are not resolved in the Gpc1 crystal structure. Therefore we have studied Gpc1 using crystallography, small-angle X-ray scattering and chromatographic approaches to elucidate the composition, structure and function of the N-glycans and the C-terminus, and also the topology of Gpc1 with respect to the membrane. The C-terminus is shown to be highly flexible in solution, but it orients the core protein transverse to the membrane, directing a surface evolutionarily conserved in Gpc1 orthologues towards the membrane, where it may interact with signalling molecules and/or membrane receptors on the cell surface, or even the enzymes involved in HS substitution in the Golgi apparatus Furthermore, the N-glycans are shown to extend the protein stability and lifetime by protection against proteolysis and aggregation.",
author = "Wael Awad and Barbara Adamczyk and Jessica {\"O}rnros and Karlsson, {Niclas G} and Katrin Mani and Logan, {Derek T}",
year = "2015",
doi = "10.1074/jbc.M115.660878",
language = "English",
volume = "290",
pages = "22991--23008",
journal = "Journal of Biological Chemistry",
issn = "1083-351X",
publisher = "ASBMB",
number = "38",