We present a protein–DNA docking benchmark containing 47 unbound–unbound test cases of which 13 are classified as easy, 22 as intermediate and 12 as difficult cases. The latter shows considerable structural rearrangement upon complex formation. DNA-specific modifications such as flipped out bases and base modifications are included. The benchmark covers all major groups of DNA-binding proteins according to the classification of Luscombe et al., except for the zipper-type group. The variety in test cases make this non-redundant benchmark a useful tool for comparison and development of protein–DNA docking methods. The benchmark is freely available as download from the internet
Protein–protein docking is the computational prediction of protein complex structure given the indiv...
Binding of proteins to particular DNA sites across the genome is a primary determinant of specificit...
The speed at which new genomes are being sequenced highlights the need for genome-wide methods capab...
We present a protein–DNA docking benchmark con-taining 47 unbound–unbound test cases of which 13 are...
The intrinsic flexibility of DNA and the difficulty of identifying its interaction surface have long...
Accurate prediction of protein–DNA complexes could provide an important stepping stone towards a tho...
International audienceWe explored the Protein DataBank (PDB) to collect protein-ssDNA structures and...
We present version 3.0 of our publicly available protein-protein docking benchmark. This update incl...
We consider the identification of interacting protein-nucleic acid partners using the rigid body doc...
Background: Protein-DNA docking is a very challenging problem in structural bioinformatics and has i...
We consider the identification of interacting protein-nucleic acid partners using the rigid body doc...
We present an updated and integrated version of our widely used protein–protein docking and binding ...
We updated our protein-protein docking benchmark to include complexes that became available since ou...
DNA-interacting proteins fulfil a vital role in the living cell. They allow the cell to quickly resp...
Summary: A protein–protein docking decoy set is built for the Dockground unbound benchmark set. The ...
Protein–protein docking is the computational prediction of protein complex structure given the indiv...
Binding of proteins to particular DNA sites across the genome is a primary determinant of specificit...
The speed at which new genomes are being sequenced highlights the need for genome-wide methods capab...
We present a protein–DNA docking benchmark con-taining 47 unbound–unbound test cases of which 13 are...
The intrinsic flexibility of DNA and the difficulty of identifying its interaction surface have long...
Accurate prediction of protein–DNA complexes could provide an important stepping stone towards a tho...
International audienceWe explored the Protein DataBank (PDB) to collect protein-ssDNA structures and...
We present version 3.0 of our publicly available protein-protein docking benchmark. This update incl...
We consider the identification of interacting protein-nucleic acid partners using the rigid body doc...
Background: Protein-DNA docking is a very challenging problem in structural bioinformatics and has i...
We consider the identification of interacting protein-nucleic acid partners using the rigid body doc...
We present an updated and integrated version of our widely used protein–protein docking and binding ...
We updated our protein-protein docking benchmark to include complexes that became available since ou...
DNA-interacting proteins fulfil a vital role in the living cell. They allow the cell to quickly resp...
Summary: A protein–protein docking decoy set is built for the Dockground unbound benchmark set. The ...
Protein–protein docking is the computational prediction of protein complex structure given the indiv...
Binding of proteins to particular DNA sites across the genome is a primary determinant of specificit...
The speed at which new genomes are being sequenced highlights the need for genome-wide methods capab...