ArticleProtein science : a publication of the Protein Society2012
NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Lipidomic Analysis Reveals Branched-Chain and Cyclic Fatty Acids fromMolecules (Basel, Switzerland) · 2024Article
- A Data-Driven Approach to Construct a Molecular Map ofVaccines · 2023Article
- Location and expression kinetics of Tc24 in different life stages of Trypanosoma cruzi.PLoS neglected tropical diseases · 2021Article
- The unusual flagellar-targeting mechanism and functions of the trypanosome ortholog of the ciliary GTPase Arl13b.Journal of cell science · 2018Article
- Characterization of Calflagin, a Flagellar Calcium-Binding Protein from Trypanosoma congolense.PLoS neglected tropical diseases · 2016Article
- Calcium-dependent membrane association of a flagellar calcium sensor does not require calcium binding.Molecular and biochemical parasitology · 2015Article
- Calcium signaling in trypanosomatid parasites.Cell calcium · 2015Review
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4 authors at 2 institutions in 1 country.
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Abstract
Flagellar calcium binding proteins are expressed in a variety of trypanosomes and are potential drug targets for Chagas disease and African sleeping sickness. The flagellar calcium binding protein calflagin of Trypanosoma brucei (called Tb24) is a myristoylated and palmitoylated EF-hand protein that is targeted to the inner leaflet of the flagellar membrane. The Tb24 protein may also interact with proteins on the membrane surface that may be different from those bound to flagellar calcium binding proteins (FCaBPs) in T. cruzi. We report here the NMR structure of Tb24 that contains four EF-hand motifs bundled in a compact arrangement, similar to the overall fold of T. cruzi FCaBP (RMSD = 1.0 Å). A cluster of basic residues (K22, K25, K31, R36, and R38) located on a surface near the N-terminal myristoyl group may be important for membrane binding. Non-conserved residues on the surface of a hydrophobic groove formed by EF2 (P91, Q95, D103, and V108) and EF4 (C194, T198, K199, Q202, and V203) may serve as a target protein binding site and could have implications for membrane target recognition.
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