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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 71 539-46 (2015)
Cited: 3 times
EuropePMC logo PMID: 25945706

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.

Articles - 4cqi mentioned but not cited (3)

  1. Structurally related but genetically unrelated antibody lineages converge on an immunodominant HIV-1 Env neutralizing determinant following trimer immunization. Aljedani SS, Liban TJ, Tran K, Phad G, Singh S, Dubrovskaya V, Pushparaj P, Martinez-Murillo P, Rodarte J, Mileant A, Mangala Prasad V, Kinzelman R, O'Dell S, Mascola JR, Lee KK, Karlsson Hedestam GB, Wyatt RT, Pancera M. PLoS Pathog 17 e1009543 (2021)
  2. A global map of the protein shape universe. Han X, Sit A, Christoffer C, Chen S, Kihara D. PLoS Comput. Biol. 15 e1006969 (2019)
  3. 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 71 539-546 (2015)




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