Understanding physical and functional interactions between molecules in living systems is crucial in many biological processes. Several powerful methods and techniques have been developed to generate molecular interaction data, focusing mainly on protein-protein interactions (PPIs). In particular, PPIs involving partially or completely unstructured regions are building blocks of regulatory and signalling networks that control cell response to external and internal cues. Exploring these interactions may help understanding a protein’s function and behavior, predicting biological processes that a protein of unknown function is involved in, and characterising protein complexes that can be used to modulate or perturb known biological processes and pathways.
The course is intended for PhD students and postdocs working in experimental biology, but scientist of all levels are welcome. Participants will be introduced to a wide variety of popular bioinformatic tools aimed at exploring and predicting PPIs. At the end of the course, participants should have an increased ability to:
Find and use information on PPIs from diverse databases.
Visualise and inspect 3D structure of PPIs and PPI networks.
Predict protein modules such as globular domains, unstructured regions and short linear motifs (LMs), from the protein sequence.
Portray the characteristics of PPIs between different types of protein modules.
Become acquainted with current strategies to target PPIs for drug design.
The course is structured in lectures and practical sessions (hands-on). Practical sessions are optional but highly advised. They will include the following applications:
Biological database searches for information on PPI data associated to any protein of interest: UniProt, MINT, ePDB/PDB, among others.
Exploration of PPI networks: STRING, STITCH, Cytoscape.
Identification of residues responsible for the physical contact between proteins in PPIs using CLUSTALX, JalView, PyMOL, PISA.
Prediction of protein interaction modules from protein sequence: using resources such as ELM, IUPRED, Anchor.
09:00 – 10:15 Considering protein interactions with smaller proteins: Protein-peptide interactions (Pierre Tufféry)
10:15 – 10:45 Coffee break
10:45 – 12:00 In silico drug design on protein-protein interactions (Olivier Sperandio)
12:00 – 14:00 Self organized lunch
14:00 – 15:30 A journey into structural disorder and induced folding in paramyxoviruses: an experimental perspective (Sonia Longhi)
15:30 – 16:00 Coffee break
16:00 – 17:00 Concluding remarks / Round table
17:00 – Social event
Registration is compulsory yet free of charge. During the registration process you’ll need to specify whether you want to take the full course, i.e. assist to both theoretical and practical sessions, or just participate in the theoretical sessions. Selected participants of the full course are encouraged to present a poster or a 5 minutes talk (flash talk) on their research subject.