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• W2589804919 abstract "Due to increasing interest in peptides as signaling modulators and drug candidates, several methods for peptide docking to their target proteins are under active development. The blind docking problem, where the peptide-binding site on the protein surface is unknown, presents one of the current challenges in the field. AnchorDock protocol was developed by Ben-Shimon and Niv to address this challenge.This protocol narrows the docking search to the most relevant parts of the conformational space. This is achieved by pre-folding the free peptide and by computationally detecting anchoring spots on the surface of the unbound protein. Multiple flexible simulated annealing molecular dynamics (SAMD) simulations are subsequently carried out, starting from pre-folded peptide conformations, constrained to the various precomputed anchoring spots.Here, AnchorDock is demonstrated using two known protein-peptide complexes. A PDZ-peptide complex provides a relatively easy case due to the relatively small size of the protein, and a typical peptide conformation and binding region; a more challenging example is a complex between USP7N-term and a p53-derived peptide, where the protein is larger, and the peptide conformation and a binding site are generally assumed to be unknown. AnchorDock returned native-like solutions ranked first and third for the PDZ and USP7 complexes, respectively. We describe the procedure step by step and discuss possible modifications where applicable." @default.
• W2589804919 created "2017-03-03" @default.
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• W2589804919 date "2017-01-01" @default.
• W2589804919 modified "2023-10-16" @default.
• W2589804919 title "AnchorDock for Blind Flexible Docking of Peptides to Proteins" @default.
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• W2589804919 doi "https://doi.org/10.1007/978-1-4939-6798-8_7" @default.
• W2589804919 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28236235" @default.
• W2589804919 hasPublicationYear "2017" @default.
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