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Article

Helical propensity in an intrinsically disordered protein accelerates ligand binding.

Angewandte Chemie (International ed. in English) - 3 Feb 2014

Iešmantavičius Vytautas, Dogan Jakob, Jemth Per, Teilum Kaare, Kjaergaard Magnus

Abstract excerpt

Many intrinsically disordered proteins fold upon binding to other macromolecules. The secondary structure present in the well-ordered complex is often formed transiently in the unbound state. The consequence of such transient structure for the binding process is, however, not clear. The activation domain of the activator for thyroid hormone and retinoid receptors (ACTR) is intrinsically disordered and folds upon...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 24449148
DOI: 10.1002/anie.201307712

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