This release is available in Spanish.
Most of the functions performed by a cell are the result of interactions between proteins, which recognise their binding partner by affinity features localized on the protein surface. There are many kinds of interactions; however, the most complicated to study from the perspective of structural biology are those which are transient. This type of interaction is brief and occurs through a large section of the protein surface- the globular domain -, and a very small section of the surface of another proteins, the so-called lineal motif or peptide. The difficulty lies in the fact that these relations are of short duration and there are few crystallized peptide structures. Researchers at the Institute for Research in Biomedicine (IRB Barcelona) have performed the first computational analysis of transient interactions between proteins in order to reveal what determines their recognition as ideal partners and have unveiled part of the molecular mechanisms involved in the specificity of this binding. The results of this study have been published in the scientific journal PLoS One.
"Knowing what determines protein-protein binding may have implications, for example, in the design of new drugs", explains Patrick Aloy, ICREA research professor at IRB Barcelona, "however, we currently know very little about this type of binding". These kinds of interactions occur mainly between proteins involved in signalling pathways and regulatory networks, and they serve to translate and transmit extracellular signals to the cell nucleus.
The context is relevant
In Patrick Aloy's Structural Biology Laboratory they have detected all interactions possible between the globular domain and peptide by exploring the 45,000 3D protein structures currently available on the international database PDB (Protein Data Base)
|Contact: Snia Armengou|
Institute for Research in Biomedicine (IRB Barcelona)