Taxonomic group: protista / Euglenozoa
(Phylum: Euglenozoa)
Host organism: Homo sapiens
Associated disease: infection due to Leishmania [ICD11:
XN8JE 
]
NCBI PubMed ID: 28876821Publication DOI: 10.1101/glycobiology.3e.012Publisher: Cold Spring Harbor (NY), Cold Spring Harbor Laboratory Press
Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Darvill AG, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger PH
Correspondence: majferguson

dundee.ac.uk
Institutions: Division of Biological Chemistry and Drug Discovery, Wellcome Trust Biocentre, College of Life Science, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom, Johns Hopkins University, Baltimore, Maryland, USA, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
Plasma membrane proteins are either peripheral proteins or integral membrane proteins. The latter include proteins that span the lipid bilayer once or several times, and another class that are covalently attached to lipids. Proteins attached to glycosylphosphatidylinositol (GPI) via their carboxyl termini are generally found in the outer leaflet of the lipid bilayer and face the extracellular environment. The GPI membrane anchor may be conveniently thought of as an alternative to the single transmembrane domain of type-1 integral membrane proteins. This chapter reviews the discovery, distribution, structure, biosynthesis, properties, and suggested functions of GPI membrane anchors and related molecules.
proteins, Glycosylphosphatidylinositol, glycobiology, GPI, membrane protein
Structure type: structural motif or average structure
Location inside paper: non-protein-linked GPI structures
Trivial name: type-2 GIPI
Compound class: glycoinositol phospholipids
Contained glycoepitopes: IEDB_130701,IEDB_141807,IEDB_144983,IEDB_144993,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 5658
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: protista / Euglenozoa
(Phylum: Euglenozoa)
Host organism: Homo sapiens
Associated disease: infection due to Leishmania [ICD11:
XN8JE 
]
NCBI PubMed ID: 28876821Publication DOI: 10.1101/glycobiology.3e.012Publisher: Cold Spring Harbor (NY), Cold Spring Harbor Laboratory Press
Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Darvill AG, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger PH
Correspondence: majferguson

dundee.ac.uk
Institutions: Division of Biological Chemistry and Drug Discovery, Wellcome Trust Biocentre, College of Life Science, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom, Johns Hopkins University, Baltimore, Maryland, USA, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
Plasma membrane proteins are either peripheral proteins or integral membrane proteins. The latter include proteins that span the lipid bilayer once or several times, and another class that are covalently attached to lipids. Proteins attached to glycosylphosphatidylinositol (GPI) via their carboxyl termini are generally found in the outer leaflet of the lipid bilayer and face the extracellular environment. The GPI membrane anchor may be conveniently thought of as an alternative to the single transmembrane domain of type-1 integral membrane proteins. This chapter reviews the discovery, distribution, structure, biosynthesis, properties, and suggested functions of GPI membrane anchors and related molecules.
proteins, Glycosylphosphatidylinositol, glycobiology, GPI, membrane protein
Structure type: structural motif or average structure
Location inside paper: non-protein-linked GPI structures
Trivial name: hybrid GIPI
Compound class: glycoinositol phospholipids
Contained glycoepitopes: IEDB_130701,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_144993,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 5658
Show glycosyltransferases
There is only one chemically distinct structure: