Fragment growing and linking used to discover inhibitors of a TB target

A paper in Angewandte Chemie International Edition on the results of a fragment-based TB drug discovery project, done in collaboration with Professor Chris Abell's group in the Department of Chemistry, is now available. CLICK HERE TO ACCESS

Our review on structural interactomics is now available

Our review entitled "Structural interactomics: informatics approaches to aid the interpretation of genetic variation and the development of novel therapeutics" in Molecular Biosystems can now be accessed online prior to full publication.
CLICK HERE TO ACCESS

Credo version 4 released

A new version of the Credo database has been released with the following changes:

  • The data generation scripts are now based on OEChem 1.7.0
  • Residues found in contact with a ligand are now compared against the polymer sequence defined in the mmCIF form to eliminate possible ligand-ligand contacts in structures where the ligand syntax is poorly defined
  • Some column data type were changed to avoid truncation of large text fields

Targeting the interaction between Rad51 and BRCA2 using fragment-based methods

Targeting the interaction between Rad51 and BRCA2 using fragment-based methods

This is the crystal structure by Dr Luca Pellegrini and co-workers of a complex between human recombinase Rad51 with the fourth BRC repeat from breast cancer associated protein BRCA2. We are applying fragment based drug discovery methods to target this protein-protein interaction with aim to develop small molecule inhibtors that can be used both as chemical tools for research and as lead compounds for eventual drug development.

PDB:
1n0w
Reference

CREDO paper published in Chemical Biology and Drug Design

CREDO: A Protein–Ligand Interaction Database for Drug Discovery

Harnessing data from the growing number of protein–ligand complexes in the Protein Data Bank is an important task in drug discovery. In order to benefit from the abundance of three-dimensional structures, structural data must be integrated with sequence as well as chemical data and the protein–small molecule interactions characterized structurally at the inter-atomic level. In this study, we present CREDO, a new publicly available database of protein–ligand interactions, which represents contacts as structural interaction fingerprints, implements novel features and is completely scriptable through its application programming interface. Features of CREDO include implementation of molecular shape descriptors with ultrafast shape recognition, fragmentation of ligands in the Protein Data Bank, sequence-to-structure mapping and the identification of approved drugs. Selected analyses of these key features are presented to highlight a range of potential applications of CREDO. The CREDO dataset has been released into the public domain together with the application programming interface under a Creative Commons license at http://www-cryst.bioc.cam.ac.uk/credo. We believe that the free availability and numerous features of CREDO database will be useful not only for commercial but also for academia-driven drug discovery programmes.

http://www3.interscience.wiley.com/journal/121654603/abstract

Syndicate content