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Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major.

Barrack KL, Fyfe PK, Finney AJ, Hunter WN - Mol. Biochem. Parasitol. (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Division of Biological Chemistry & Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.

No MeSH data available.


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Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major.

Barrack KL, Fyfe PK, Finney AJ, Hunter WN - Mol. Biochem. Parasitol. (2015)

© Copyright Policy - CC BY
Related In: Results  -  Collection

License
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getmorefigures.php?uid=PMC4539340&req=5

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Division of Biological Chemistry & Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.

No MeSH data available.