Projects per year
Abstract
Tubulin-binding cofactor A (TBCA) participates in microtubule formation, a key process in eukaryotic biology to create the cytoskeleton. There is little information on how TBCA might interact with β-tubulin en route to microtubule biogenesis. To address this, the protozoan Leishmania major was targeted as a model system. The crystal structure of TBCA and comparisons with three orthologous proteins are presented. The presence of conserved features infers that electrostatic interactions that are likely to involve the C-terminal tail of β-tubulin are key to association. This study provides a reagent and template to support further work in this area.
Original language | English |
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Pages (from-to) | 539-546 |
Number of pages | 8 |
Journal | Acta Crystallographica Section F: Structural Biology Communications |
Volume | 71 |
Issue number | 5 |
DOIs | |
Publication status | Published - May 2015 |
Keywords
- Chaperone
- Helical fold
- Molecular parasitology - advances in biology and supporting drug discovery
- Protein-protein interactions
- Selenomethionine
- Tubulin-binding protein
Fingerprint Dive into the research topics of 'The structure of tubulin-binding cofactor A from <i>Leishmania major</i> infers a mode of association during the early stages of microtubule assembly'. Together they form a unique fingerprint.
Projects
- 2 Finished
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State-of-the-Art Facilities for Structural Biology at the University of Dundee
Hunter, B., Lilley, D., Owen-Hughes, T., Wyatt, P. & van Aalten, D.
1/03/12 → 28/02/17
Project: Research