(1)H, (13)C and (15)N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein - Archive ouverte HAL Access content directly
Journal Articles Biomolecular NMR Assignments Year : 2011

(1)H, (13)C and (15)N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein

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Abstract

Engrailed 2 is a transcription factor belonging to the class of homeoproteins. These proteins possess a 60-residue DNA binding globular domain and play an important role in the early stages of development. We expressed and purified a 13.4 kDa fragment of Engrailed 2, which comprises a 54-residue N-terminal extension in addition to the homeodomain region. Almost all backbone and side-chain resonances have been assigned. The weak dispersion in the proton dimension of the (1)H-(15)N HSQC spectrum indicates the presence of disordered regions that do not belong to the homeodomain. This work is a first step toward the NMR investigation of the structure and dynamics of Engrailed 2 protein that contains a well-structured globular domain and partially disordered regions.

Dates and versions

hal-00632165 , version 1 (13-10-2011)

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Rafal Augustyniak, Stéphane Balayssac, Fabien Ferrage, Geoffrey Bodenhausen, Olivier Lequin. (1)H, (13)C and (15)N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein. Biomolecular NMR Assignments, 2011, 5 (2), pp.229-31. ⟨10.1007/s12104-011-9306-5⟩. ⟨hal-00632165⟩
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