INB Integrated platform for macromolecular flexibility
Biological function is largely based on molecular recognition. Biological macromolecules interact to each other following strict rules on the complementarity of 3D structures and interactions. The understanding of molecular recognition has been based traditionally on the analysis of static models of protein and nucleic acids 3D structures as found in the Protein Data Bank. However, molecular recognition requires precise adjustments of the structures to optimize the binding, what is possible due to the intrinsic flexibility of biological macromolecules, but very difficult to follow using static pictures of those structures. Although some information about flexibility and induced fit could be extracted from the set of conformations available in PDB, onty theoretical methods can draw a full picture of the phenomenon. A series of tools and databases related to flexibility have been developed to offer an integrated approach to study flexibility.
Modesto Orozco, Laura Orellana, Adam Hospital, Athi Naganathan, Agustí Emperador, Oliver Carrillo, Josep Lluís Gelpí
Coarse-grained representation of protein flexibility. Foundations, successes, and shortcomings.
Adv. Protein Chem. Struct. Biol. 2011;85:183-215.
Laia Codó, Genís Bayarri, Javier Alvarez Cid-Fuentes, Javier Conejero, Adam Hospital, Romina Royo, Dmitry Repchevsky, Marco Pasi, Athina Meletiou, Mark D. McDowall, Fatima Reham, José A. Alcantara, Brian Jimenez-Garcia, Jürgen Walther, Ricard Illa, François Serra, Michael Goodstadt, David Castillo, Satish Sati, Diana Buitrago, Isabelle Brun-Heath, Juan Fernandez-Recio, Giacomo Cavalli, Marc Marti-Renom, Andrew Yates, Charles A. Laughton, Rosa M. Badia, Modesto Orozco, Josep Ll. Gelpí
MuGVRE. A virtual research environment for 3D/4D genomics