Functional identification of alpha 1-giardin as an annexin of Giardia lamblia

Autor(en): Bauer, B
Engelbrecht, S
Bakker-Grunwald, T
Scholze, H
Stichwörter: annexin; ANTICOAGULANT; BINDING PROTEINS; CALCIUM; calcium binding; Giardia lamblia; giardin; Microbiology; phospholipid binding
Erscheinungsdatum: 1999
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEMS MICROBIOLOGY LETTERS
Volumen: 173
Ausgabe: 1
Startseite: 147
Seitenende: 153
Zusammenfassung: 
A protein with a relative molecular mass of 31 kDa was specifically extracted by EGTA from a detergent-insoluble fraction of Giardia lamblia. N-terminal sequencing showed this protein to be identical to alpha 1-giardin, a component of the ventral disc which, based on its predicted amino acid sequence, has been classified as annexin XIX. Purified alpha 1-giardin associated with multilamellar phosphatidyl serine-containing vesicles in a Ca2+-dependent manner, confirming that it is a functional annexin. Molecular modelling of the amino acid sequence of the giardial annexin into the X-ray structure of annexin V suggests that the Ca2+-binding sites, which, as in other annexins, are all located on the convex surface of the molecule, are of the low-affinity type III. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
ISSN: 03781097
DOI: 10.1111/j.1574-6968.1999.tb13496.x

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