Structural highlights
Publication Abstract from PubMed
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 beta-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 beta-tubulin are key to association. This study provides a reagent and template to support further work in this area.
The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly.,Barrack KL, Fyfe PK, Hunter WN Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):539-46. doi:, 10.1107/S2053230X15000990. Epub 2015 Apr 21. PMID:25945706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barrack KL, Fyfe PK, Hunter WN. The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly. Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):539-46. doi:, 10.1107/S2053230X15000990. Epub 2015 Apr 21. PMID:25945706 doi:http://dx.doi.org/10.1107/S2053230X15000990
