Structure and function of GPI-anchored surface proteins of Trypanosoma brucei.
While proteins modified at their COOH-terminal end by a glycosylphosphatidylinositol (GPI) membrane anchor have been found as minor components in many eukaryotic cells, they dominate surface constituents of several parasitic protozoa. In this article, GPI-anchored proteins of Trypanosoma brucei are discussed.
Overath
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Max-Planck-Institut für Biologie, Abteilung Membranbiochemie, Tübingen, Germany.
Steverding
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Chaudhri
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Stierhof
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Ziegelbauer
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D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology*; D017261:Glycosylphosphatidylinositols / Q000737:chemistry* / Q000502:physiology; D013329:Structure-Activity Relationship; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000502:physiology; D014643:Variant Surface Glycoproteins, Trypanosoma / Q000737:chemistry / Q000502:physiology*
D002352:Carrier Proteins; D017261:Glycosylphosphatidylinositols; D014643:Variant Surface Glycoproteins, Trypanosoma