1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A |
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Authors: | Sophie Feuerstein Zsófia Solyom Amine Aladağ Silke Hoffmann Dieter Willbold Bernhard Brutscher |
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Affiliation: | 1. Institut de Biologie Structurale, Université Grenoble 1, 41 rue Jules Horowitz, 38027, Grenoble Cedex 1, France 2. Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA), Grenoble, France 3. Centre National de Recherche Scientifique (CNRS), Grenoble, France 4. Institute for Complex Systems (ISC-6) Structural Biochemistry, Forschungszentrum Jülich, 52425, Jülich, Germany 5. Institut für Physikalische Biologie, Heinrich-Heine-Universit?t, 40225, Düsseldorf, Germany
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Abstract: | Non-structural protein 5A (NS5A) plays an important role in the life cycle of hepatitis C virus. This proline-rich phosphoprotein is organized into three domains. Besides its role in virus replication and virus assembly, NS5A is involved in a variety of cellular regulation processes. Recent studies on domain 2 and 3 revealed that both belong to the class of intrinsically disordered proteins as they adopt a natively unfolded state. In particular, domain 2 together with its vicinal regions is responsible for NS5A’s multiple interactions with other proteins necessary for virus persistence. The low chemical shift dispersion observed for instrinsically disordered proteins presents a challenge for NMR spectroscopy. Here we report sequential resonance assignment of a 179-residue fragment of NS5A, comprising the entire domain 2, using a set of sensitivity and resolution optimized 3D correlation experiments, as well as amino-acid-type editing in 1H-15N correlation spectra. Our assignment reveals the presence of several segments with high propensity to form α-helical structure that may be of importance to the function of this protein fragment as a versatile interaction platform. |
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