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Title: Structure of the N-terminal domain of the protein Expansion: an 'Expansion' to the Smad MH2 fold
Author: Beich-Frandsen, M.
Aragón Altarriba, Eric
Llimargas i Casanova, Marta
Benach, Jordi
Riera i Escalé, Antoni
Pous, Joan
Macias, Maria Jesus
Keywords: Proteïnes
Issue Date: 22-Jan-2015
Publisher: International Union of Crystallography
Abstract: Gene-expression changes observed in Drosophila embryos after inducing the transcription factor Tramtrack led to the identification of the protein Expansion. Expansion contains an N-terminal domain similar in sequence to the MH2 domain characteristic of Smad proteins, which are the central mediators of the effects of the TGF- signalling pathway. Apart from Smads and Expansion, no other type of protein belonging to the known kingdoms of life contains MH2 domains. To compare the Expansion and Smad MH2 domains, the crystal structure of the Expansion domain was determined at 1.6 A˚ resolution, the first structure of a non-Smad MH2 domain to be characterized to date. The structure displays the main features of the canonical MH2 fold with two main differences: the addition of an -helical region and the remodelling of a protein-interaction site that is conserved in the MH2 domain of Smads. Owing to these differences, to the new domain was referred to as N-MH2. Despite the presence of the N-MH2 domain, Expansion does not participate in TGF- signalling; instead, it is required for other activities specific to the protostome phyla. Based on the structural similarities to the MH2 fold, it is proposed that the N-MH2 domain should be classified as a new member of the Smad/FHA superfamily. 1.
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It is part of: Acta Crystallographica Section C: Crystal Structure Communications, 2015, vol. D71, p. 844-853
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ISSN: 0108-2701
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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