Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2003-12

AUTHORS

Marcin Grynberg, Lukasz Jaroszewski, Adam Godzik

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. More... »

PAGES

46

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1471-2105-4-46

DOI

http://dx.doi.org/10.1186/1471-2105-4-46

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028832522

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/14536023


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