ArticleMolecular and biochemical parasitology2015
Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major.
Article in Molecular and biochemical parasitology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 5 citations in OpenAlex.
- Brownian Dynamics Simulations of Biological Molecules.Trends in chemistry · 2019Article
- Article
- The C-terminal dimerization motif of cyclase-associated protein is essential for actin monomer regulation.The Biochemical journal · 2016Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Tubulin-binding cofactor C stimulates GTPase activity and contributes to the release of the heterodimeric α/β-tubulin from a super-complex of tubulin monomers and two ancillary cofactors. We have determined the 2.2 Å resolution crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major based on single wavelength anomalous dispersion measurements targeting a selenomethionine derivative. Although previously predicted to consist of two domains the structure is best described as a single domain dominated by a right-handed β-helix of five turns that form a triangular prism. One face of the prism is covered by the C-terminal residues leaving another face solvent exposed. Comparisons with an orthologous human GTPase activating protein match key residues involved in binding nucleotide and identify the face of the β-helix fold likely involved in interacting with the β-tubulin:GTP complex.
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