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BMC Bioinformatics. 2003 Oct 10;4:46.

Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization.

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  • 1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego St, 02-106 Warsaw, Poland. marcin@ljcrf.edu

Abstract

BACKGROUND:

The correct folding and dimerization of tubulins, before their addition to the microtubular structure, needs a group of conserved proteins called cofactors A to E. The biochemical analysis of cofactors gave an insight to their general functions, however not much is known about the domain structure and detailed, molecular function of these proteins.

RESULTS:

Combining modelling and fold prediction tools, we present 3D models of all cofactors, including several previously unannotated domains of cofactors B-E. Apart from the new HEAT and Armadillo domains in cofactor D and an unusual spectrin-like domain in cofactor C, we have identified a new subfamily of ubiquitin-like domains in cofactors B and E. Together, these observations provide a reliable, molecular level model of cofactor complex.

CONCLUSION:

Distant homology searches allowed the identification of unknown regions of cofactors as self-reliant domains and allow us to present a detailed hypothesis of how a cofactor complex performs its function.

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