Experimental and bioinformatic characterization of CaBP2933 an EF-Hand protein of Giardia intestinalis
Model of 3D structure for calcium binding protein CaBP2933. The two EF-Hand domains are shown, Ca2+ ions are depicted as gray balls. [Display omitted] •The exclusive protein CaBP2933 of G. intestinalis it is able binding calcium.•CaBP2933 protein was initially incorrectly named “programmed cell deat...
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Veröffentlicht in: | Molecular and biochemical parasitology 2017-06, Vol.214, p.65-68 |
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Sprache: | eng |
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Zusammenfassung: | Model of 3D structure for calcium binding protein CaBP2933. The two EF-Hand domains are shown, Ca2+ ions are depicted as gray balls.
[Display omitted]
•The exclusive protein CaBP2933 of G. intestinalis it is able binding calcium.•CaBP2933 protein was initially incorrectly named “programmed cell death protein-like protein”.•The encystation stimulus influences the subcellular location of CaBP2933.•CaBP2933 interacting with the motor protein kinesin-3.
Giardia intestinalis is a parasite that inhabits the small intestine of humans. This parasite is a divergent eukaryote with a compact genome. The calcium ion is an essential messenger in cell signaling. Calcium’s role as a messenger is mediated through calcium-binding proteins (CaBPs) that decode the message. The most important family of CaBPs is the EF-Hand protein family. In this study we have explored the role of EF-Hand protein CaBP2933. We analyzed its location, confirmed its ability to bind calcium and identified some of its interacting proteins. Take together our results suggest that CaBP2933 is involved in vesicular trafficking during encystation, via an interaction with kinesin-3 motor protein. |
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ISSN: | 0166-6851 1872-9428 |
DOI: | 10.1016/j.molbiopara.2017.03.010 |