Parent Category: Laboratoires Published: Monday, 27 June 2016

Structure and Function of Highly Flexible Proteins





 CBS - UMR 5048/U1054

 29, rue de Navacelles, 34090 Montpellier


Phone: +33 4 67 41 79 12






The aim of the group is the characterization of the structure-dynamics-function relationship of biomolecular systems with important levels of flexibility. Intrinsically Disordered Proteins (IDPs), multidomain proteins, allosteric enzymes, and proteins with low-complexity regions focus the interest of our group. Our team addresses these challenges by integrative approaches where structural and dynamic information derived from different structural biology and biophysical methods are integrated into computational strategies to achieve more complete models of the systems of interest. The group hosts the expertise in Nuclear Magnetic Resonance (Nathalie Sibille), Small-Angle X-ray Scattering, molecular modelling, and advanced tools in biochemistry and molecular biology (Frédéric Allemand).

We are developing strategies to obtain structural information from flexible proteins hosting low-complexity regions, which cannot be studied nowadays, by applying molecular and chemical biology tools. We are also designing approaches to couple advanced computational methods to further understand the structure and dynamics of biomolecular complexes. We apply these approaches to unravel relevant biophysical phenomena such as molecular recognition, transient interactions, allosterism, and amyloidogenesis that are directly involved in signal transduction, gene expression, homeostasis, and neurodegeneration. The protein huntingtin (involved in Huntington’s disease), disordered C-terminal regions of GPCRs (involved in the arresting signalling pathway), and the regulation of hormonal nuclear receptors are the three main scientific projects of the team.


Keywords: Intrinsically Disordered Proteins, Low-Complexity Regions, protein structure/dynamics, Nuclear Magnetic Resonance, Small-Angle X-ray Scattering, molecular modelling.


Main publications

  • Herranz-Trillo, F.; Groenning, M.; van Maarschalkerweerd, A.; Tauler, R.; Vestergaard, B.; Bernadó, P. Structural Analysis of Multicomponent Amyloid Systems by Chemometric SAXS Data Decomposition. Structure, 2017, 25, 5-15.
  • Cordeiro, T.N.; Chen, P.C.; De Biasio, A.; Sibille, N.; Blanco, F.J.; Hub, J.S.; Crehuet, R.; Bernadó, P. Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly. Nucleic Acids Research 2017, 45, 1501-1515.
  • Cordeiro, T.N.; Herranz-Trillo, F.; Urbanek, A.; Estaña, A.; Cortés, J.; Sibille, N.; Bernadó, P. Small-Angle X-ray Scattering of disordered proteins and their complexes. Current Opinion in Structural Biology, 2016, 42, 15-23.
  • De Biasio, A.; de Opakua, A.I.; Mortuza, G.B.; Molina, R.; Cordeiro, T.N.; Castillo, F.; Villate, M.; Merino, N.; Delgado, S.; Gil-Cartón, D.; Luque, I.; Diercks, T.; Bernadó, P.; Montoya, G.; Blanco, F.J. Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. Nature Communications 2015, 6, 6439.
  • Pérez-Cano, L.; Eliahoo, E.; Lasker, K.; Wolfson, H.; Glaser, F.; Manor, H.; Bernadó, P.; Fernández-Recio, J. Conformational transitions in human translin enable nucleic acid binding. Nucleic Acids Research 2013, 41, 9956-9966.
  • Sibille, N.; Bernadó, P. Structural Characterization of Intrinsically Disordered Proteins by the Combined Use of NMR and SAXS. Biochemical Society Transactions, 2012, 40, 955-962.
  • Rubio-Cosials, A.; Sidow, J.F.; Jiménez-Menéndez, N.; Fernández-Millán, P.; Montoya, J.; Jacobs, H.T.; Coll, M.; Bernadó, P.; Solà, M. Human mitochondrial transcription factor A induces a U-turn structure in the light stranded promoter. Nature Structural & Molecular Biology, 2011, 18, 1281-1289.
  • Bernadó, P.; Blackledge, M. Proteins in dynamic equilibrium. Nature, 2010, 468, 1046-1048.
  • Bernadó, P.; Mylonas, E.; Petoukhov, M.V.; Blackledge, M.; Svergun, D.I. Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering. Journal of the American Chemical Society, 2007, 129, 5656-5664.
  • Bernadó, P.; Blanchard, L.; Timmins, P.; Marion, D.; Ruigrok, R.H.W.; Blackledge, M. A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proceedings of the National Academy of Sciences of the USA 2005, 102, 17002-17007.

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