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Updated: May 9, 2026

Dissection and Immunostaining of Imaginal Discs from Drosophila melanogaster
Published on: September 20, 2014
The structure of the TOG-like domain of Drosophila melanogaster Mast/Orbit
Teresa De la Mora-Rey1, Brian D Guenther, Barry C Finzel
1Department of Medicinal Chemistry, University of Minnesota, 308 Harvard Street SE, 8-101 Weaver-Densford Hall, Minneapolis, MN 55455, USA.
Abstract:
Mast/Orbit is a nonmotor microtubule-associated protein (MAP) present in Drosophila melanogaster that reportedly binds microtubules at the plus end and is essential for mitosis. Sequence analysis has shown that the N-terminal domain (Mast-M1) resembles TOG domains from the Dis1-TOG family of proteins and stands as a representative of one of the three subclasses of divergent TOG-like domains (TOGL1) that includes human CLASP1. The crystal structure of Mast-M1 has been determined at 2.0 Å resolution and provides the first detailed structural description of any TOG-like domain. The structure confirms that Mast-M1 adopts a similar fold to the previously described Dis1-TOG domains of microtubule-binding proteins. A comparison with three known TOG-domain structures from XMAP215/Dis1 family members exposes significant differences between Mast-M1 and other TOG-domain structures in key residues at the proposed tubulin-binding edge.
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