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Open AccessJournal ArticleDOI

PatchDock and SymmDock: servers for rigid and symmetric docking

TLDR
Two freely available web servers for molecular docking that perform structure prediction of protein–protein and protein–small molecule complexes and the SymmDock method predicts the structure of a homomultimer with cyclic symmetry given theructure of the monomeric unit are described.
Abstract
Here, we describe two freely available web servers for molecular docking. The PatchDock method performs structure prediction of protein-protein and protein-small molecule complexes. The SymmDock method predicts the structure of a homomultimer with cyclic symmetry given the structure of the monomeric unit. The inputs to the servers are either protein PDB codes or uploaded protein structures. The services are available at http://bioinfo3d.cs.tau.ac.il. The methods behind the servers are very efficient, allowing large-scale docking experiments.

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Citations
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Journal ArticleDOI

The ClusPro web server for protein-protein docking.

TL;DR: This protocol describes the use of the various options, the construction of auxiliary restraints files, the selection of the energy parameters, and the analysis of the results of the ClusPro server.
Journal ArticleDOI

ZDOCK server: interactive docking prediction of protein-protein complexes and symmetric multimers.

TL;DR: This paper presents a user-friendly protein docking server, based on the rigid-body docking programs ZDOCK and M-ZDOCK, to predict structures of protein-protein complexes and symmetric multimers, and provides options for users to guide the scoring and the selection of output models.
Journal ArticleDOI

The HADDOCK web server for data-driven biomolecular docking

TL;DR: The HADDOCK web server protocol is presented, facilitating the modeling of biomolecular complexes for a wide community, and has access to the resources of a dedicated cluster and of the e-NMR GRID infrastructure.
Journal ArticleDOI

Software for molecular docking: a review

TL;DR: Docking against homology-modeled targets also becomes possible for proteins whose structures are not known, and the druggability of the compounds and their specificity against a particular target can be calculated for further lead optimization processes.
Journal ArticleDOI

GRAMM-X public web server for protein-protein docking

TL;DR: GRAMM-X and its web interface extend the original GRAMM Fast Fourier Transformation methodology by employing smoothed potentials, refinement stage, and knowledge-based scoring and frees users from complex installation of database-dependent parallel software and maintaining large hardware resources needed for protein docking simulations.
References
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Journal ArticleDOI

Development and validation of a genetic algorithm for flexible docking.

TL;DR: GOLD (Genetic Optimisation for Ligand Docking) is an automated ligand docking program that uses a genetic algorithm to explore the full range of ligand conformational flexibility with partial flexibility of the protein, and satisfies the fundamental requirement that the ligand must displace loosely bound water on binding.
Journal ArticleDOI

Solvent-Accessible Surfaces of Proteins and Nucleic Acids

TL;DR: A method is presented for analytically calculating a smooth, three-dimensional contour about a molecule, which has been applied in enzymology, rational drug design, immunology, and understanding DNA base sequence recognition.
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Analytical molecular surface calculation

TL;DR: In this paper, a computer algorithm is presented for calculating the part of the van der Waals surface of a molecule that is accessible to solvent, where the solvent molecule is modeled by a sphere and a sphere is, in effect, rolled over the molecule to generate a smooth outer surface contour.
Journal ArticleDOI

A geometric approach to macromolecule-ligand interactions

TL;DR: A method to explore geometrically feasible alignments of ligands and receptors of known structure and finds distinctly different geometries that provide good steric fits seems well-suited for generating starting conformations for energy refinement programs and interactive computer graphics routines.
Journal ArticleDOI

Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations.

TL;DR: A new method to predict protein-protein complexes from the coordinates of the unbound monomer components using a low-resolution, rigid-body, Monte Carlo search followed by simultaneous optimization of backbone displacement and side-chain conformations using Monte Carlo minimization is presented.
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