Conformational analysis of the partially disordered measles virus NTAIL-XD complex by SDSL EPR spectroscopy

Aleh Kavalenka, Iztok Urbančič, Valérie Belle, Sabrina Rouger, Stéphanie Costanzo, Sandra Kure, André Fournel, Sonia Longhi, Bruno Guigliarelli, Janez Strancar
Biophysical journal, March 2010; doi: 10.1016/j.bpj.2009.11.036 (read more here).

In brief

To characterize the structure of dynamic protein systems, such as partly disordered protein complexes, we propose a novel approach that relies on a combination of site-directed spin-labeled electron paramagnetic resonance spectroscopy and modeling of local rotation conformational spaces. We applied this approach to the intrinsically disordered C-terminal domain of the measles virus nucleoprotein and provided a mechanistic explanation for the high affinity of the binding reaction between the measles virus and the viral phosphoprotein.