Software and Databases for Protein-Protein Docking.

Fast Fourier transform Monte Carlo PPI Protein bioinformatics Protein databases Protein–protein docking Protein–protein interactions Protein–protein interface

Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2024
Historique:
medline: 11 7 2024
pubmed: 11 7 2024
entrez: 10 7 2024
Statut: ppublish

Résumé

Protein-protein interactions (PPIs) provide valuable insights for understanding the principles of biological systems and for elucidating causes of incurable diseases. One of the techniques used for computational prediction of PPIs is protein-protein docking calculations, and a variety of software has been developed. This chapter is a summary of software and databases used for protein-protein docking.

Identifiants

pubmed: 38987467
doi: 10.1007/978-1-0716-3985-6_8
doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

129-138

Informations de copyright

© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Bonetta L (2010) Interactome under construction. Nature 468:851–852. https://doi.org/10.1038/468851a
doi: 10.1038/468851a pubmed: 21150998
Kuzmanov U, Emili A (2013) Protein-protein interaction networks: probing disease mechanisms using model systems. Genome Med 5:37. https://doi.org/10.1186/gm441
doi: 10.1186/gm441 pubmed: 23635424 pmcid: 3706760
Kaczor AA, Bartuzi D, Stępniewski TM et al (2018) Protein–protein docking in drug design and discovery. Methods Mol Biol 1762:285–305
doi: 10.1007/978-1-4939-7756-7_15 pubmed: 29594778
Wodak SJ, Vlasblom J, Turinsky AL, Pu S (2013) Protein–protein interaction networks: the puzzling riches. Curr Opin Struct Biol 23:941–953. https://doi.org/10.1016/j.sbi.2013.08.002
doi: 10.1016/j.sbi.2013.08.002 pubmed: 24007795
Nooren IMA (2003) NEW EMBO MEMBER’S REVIEW: diversity of protein-protein interactions. EMBO J 22:3486–3492. https://doi.org/10.1093/emboj/cdg359
doi: 10.1093/emboj/cdg359 pubmed: 12853464 pmcid: 165629
Janin J, Bahadur RP, Chakrabarti P (2008) Protein–protein interaction and quaternary structure. Q Rev Biophys 41:133–180. https://doi.org/10.1017/S0033583508004708
doi: 10.1017/S0033583508004708 pubmed: 18812015
Janin J, Henrick K, Moult J et al (2003) CAPRI: a critical assessment of PRedicted interactions. Proteins Struct Funct Genet 52:2–9. https://doi.org/10.1002/prot.10381
doi: 10.1002/prot.10381 pubmed: 12784359
Fernández-Recio J, Totrov M, Abagyan R (2003) ICM-DISCO docking by global energy optimization with fully flexible side-chains. Proteins Struct Funct Bioinform 52:113–117. https://doi.org/10.1002/prot.10383
doi: 10.1002/prot.10383
Fernández-Recio J, Abagyan R, Totrov M (2005) Improving CAPRI predictions: optimized desolvation for rigid-body docking. Proteins Struct Funct Bioinform 60:308–313. https://doi.org/10.1002/prot.20575
doi: 10.1002/prot.20575
Katchalski-Katzir E, Shariv I, Eisenstein M et al (1992) Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc Natl Acad Sci 89:2195–2199. https://doi.org/10.1073/pnas.89.6.2195
doi: 10.1073/pnas.89.6.2195 pubmed: 1549581 pmcid: 48623
Desta IT, Porter KA, Xia B et al (2020) Performance and its limits in rigid body protein-protein docking. Structure 28:1071–1081.e3. https://doi.org/10.1016/j.str.2020.06.006
doi: 10.1016/j.str.2020.06.006 pubmed: 32649857 pmcid: 7484347
Pozzati G, Kundrotas P, Elofsson A (2022) Scoring of protein–protein docking models utilizing predicted interface residues. Proteins Struct Funct Bioinform 90:1493–1505. https://doi.org/10.1002/prot.26330
doi: 10.1002/prot.26330
Bernstein FC, Koetzle TF, Williams GJB et al (1977) The protein data bank: a computer-based archival file for macromolecular structures. J Mol Biol 112:535–542. https://doi.org/10.1016/S0022-2836(77)80200-3
doi: 10.1016/S0022-2836(77)80200-3 pubmed: 875032
Gonzalez O (2013) Protein–protein interaction databases. In: Encyclopedia of systems biology. Springer, New York, pp 1786–1790
doi: 10.1007/978-1-4419-9863-7_1046
Stacey RG, Skinnider MA, Chik JHL, Foster LJ (2018) Context-specific interactions in literature-curated protein interaction databases. BMC Genomics 19:758. https://doi.org/10.1186/s12864-018-5139-2
doi: 10.1186/s12864-018-5139-2 pubmed: 30340458 pmcid: 6194712
Nemethy G, Gibson KD, Palmer KA et al (1992) Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides. J Phys Chem 96:6472–6484. https://doi.org/10.1021/j100194a068
doi: 10.1021/j100194a068
Cardozo T, Totrov M, Abagyan R (1995) Homology modeling by the ICM method. Proteins Struct Funct Genet 23:403–414. https://doi.org/10.1002/prot.340230314
doi: 10.1002/prot.340230314 pubmed: 8710833
Ma B, Elkayam T, Wolfson H, Nussinov R (2003) Protein–protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc Natl Acad Sci 100:5772–5777. https://doi.org/10.1073/pnas.1030237100
doi: 10.1073/pnas.1030237100 pubmed: 12730379 pmcid: 156276
Jones S, Thornton JM (1997) Prediction of protein-protein interaction sites using patch analysis 1 1Edited by G. von Heijne. J Mol Biol 272:133–143. https://doi.org/10.1006/jmbi.1997.1233
doi: 10.1006/jmbi.1997.1233 pubmed: 9299343
Fernandez-Recio J, Totrov M, Skorodumov C, Abagyan R (2004) Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins Struct Funct Bioinform 58:134–143. https://doi.org/10.1002/prot.20285
doi: 10.1002/prot.20285
Fischer D, Lin SL, Wolfson HL, Nussinov R (1995) A geometry-based suite of moleculardocking processes. J Mol Biol 248:459–477. https://doi.org/10.1016/S0022-2836(95)80063-8
doi: 10.1016/S0022-2836(95)80063-8 pubmed: 7739053
Abagyan R, Totrov M, Kuznetsov D (1994) ICM?A new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J Comput Chem 15:488–506. https://doi.org/10.1002/jcc.540150503
doi: 10.1002/jcc.540150503
Totrov M, Abagyan R (1994) Detailed ab initio prediction of lysozyme–antibody complex with 1.6 Å accuracy. Nat Struct Mol Biol 1:259–263. https://doi.org/10.1038/nsb0494-259
doi: 10.1038/nsb0494-259
Arnautova YA, Abagyan R, Totrov M (2018) Protein-RNA docking using ICM. J Chem Theory Comput 14:4971–4984. https://doi.org/10.1021/acs.jctc.8b00293
doi: 10.1021/acs.jctc.8b00293 pubmed: 30016588
Moal IH, Torchala M, Bates PA, Fernández-Recio J (2013) The scoring of poses in protein-protein docking: current capabilities and future directions. BMC Bioinform 14:286. https://doi.org/10.1186/1471-2105-14-286
doi: 10.1186/1471-2105-14-286
Liu J, Wang R (2015) Classification of current scoring functions. J Chem Inf Model 55:475–482. https://doi.org/10.1021/ci500731a
doi: 10.1021/ci500731a pubmed: 25647463
Neves MAC, Totrov M, Abagyan R (2012) Docking and scoring with ICM: the benchmarking results and strategies for improvement. J Comput Aided Mol Des 26:675–686. https://doi.org/10.1007/s10822-012-9547-0
doi: 10.1007/s10822-012-9547-0 pubmed: 22569591 pmcid: 3398187
Oughtred R, Rust J, Chang C et al (2021) The BioGRID database: a comprehensive biomedical resource of curated protein, genetic, and chemical interactions. Protein Sci 30:187–200. https://doi.org/10.1002/pro.3978
doi: 10.1002/pro.3978 pubmed: 33070389
Bader GD (2001) BIND—the biomolecular interaction network database. Nucleic Acids Res 29:242–245. https://doi.org/10.1093/nar/29.1.242
doi: 10.1093/nar/29.1.242 pubmed: 11125103 pmcid: 29820
Xenarios I (2000) DIP: the database of interacting proteins. Nucleic Acids Res 28:289–291. https://doi.org/10.1093/nar/28.1.289
doi: 10.1093/nar/28.1.289 pubmed: 10592249 pmcid: 102387
Hermjakob H (2004) IntAct: an open source molecular interaction database. Nucleic Acids Res 32:452D–455D. https://doi.org/10.1093/nar/gkh052
doi: 10.1093/nar/gkh052
Orchard S, Ammari M, Aranda B et al (2014) The MIntAct project—IntAct as a common curation platform for 11 molecular interaction databases. Nucleic Acids Res 42:D358–D363. https://doi.org/10.1093/nar/gkt1115
doi: 10.1093/nar/gkt1115 pubmed: 24234451
Negi SS, Schein CH, Oezguen N et al (2007) InterProSurf: a web server for predicting interacting sites on protein surfaces. Bioinformatics 23:3397–3399. https://doi.org/10.1093/bioinformatics/btm474
doi: 10.1093/bioinformatics/btm474 pubmed: 17933856
Chatr-aryamontri A, Ceol A, Palazzi LM et al (2007) MINT: the molecular INTeraction database. Nucleic Acids Res 35:D572–D574. https://doi.org/10.1093/nar/gkl950
doi: 10.1093/nar/gkl950 pubmed: 17135203
Pagel P, Kovac S, Oesterheld M et al (2005) The MIPS mammalian protein-protein interaction database. Bioinformatics 21:832–834. https://doi.org/10.1093/bioinformatics/bti115
doi: 10.1093/bioinformatics/bti115 pubmed: 15531608
Zhou Y, Chen H, Li S, Chen M (2021) mPPI: a database extension to visualize structural interactome in a one-to-many manner. Database 2021. https://doi.org/10.1093/database/baab036
Chen YC, Chen Y-H, Wright JD, Lim C (2022) PPI-hotspot DB: database of protein–protein interaction hot spots. J Chem Inf Model 62:1052–1060. https://doi.org/10.1021/acs.jcim.2c00025
doi: 10.1021/acs.jcim.2c00025 pubmed: 35147037
Moreira IS, Koukos PI, Melo R et al (2017) SpotOn: high accuracy identification of protein-protein Interface hot-spots. Sci Rep 7:8007. https://doi.org/10.1038/s41598-017-08321-2
doi: 10.1038/s41598-017-08321-2 pubmed: 28808256 pmcid: 5556074
Szklarczyk D, Gable AL, Nastou KC et al (2021) The STRING database in 2021: customizable protein–protein networks, and functional characterization of user-uploaded gene/measurement sets. Nucleic Acids Res 49:D605–D612. https://doi.org/10.1093/nar/gkaa1074
doi: 10.1093/nar/gkaa1074 pubmed: 33237311
Morris GM, Huey R, Lindstrom W et al (2009) AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30:2785–2791. https://doi.org/10.1002/jcc.21256
doi: 10.1002/jcc.21256 pubmed: 19399780 pmcid: 2760638
Zacharias M (2003) Protein-protein docking with a reduced protein model accounting for side-chain flexibility. Protein Sci 12:1271–1282. https://doi.org/10.1110/ps.0239303
doi: 10.1110/ps.0239303 pubmed: 12761398 pmcid: 2323887
Kozakov D, Hall DR, Xia B et al (2017) The ClusPro web server for protein–protein docking. Nat Protoc 12:255–278. https://doi.org/10.1038/nprot.2016.169
doi: 10.1038/nprot.2016.169 pubmed: 28079879 pmcid: 5540229
Chaudhury S, Berrondo M, Weitzner BD et al (2011) Benchmarking and analysis of protein docking performance in Rosetta v3.2. PLoS One 6:e22477. https://doi.org/10.1371/journal.pone.0022477
doi: 10.1371/journal.pone.0022477 pubmed: 21829626 pmcid: 3149062
Roberts VA, Thompson EE, Pique ME et al (2013) DOT2: macromolecular docking with improved biophysical models. J Comput Chem 34:1743–1758. https://doi.org/10.1002/jcc.23304
doi: 10.1002/jcc.23304 pubmed: 23695987 pmcid: 4370774
Ramírez-Aportela E, López-Blanco JR, Chacón P (2016) FRODOCK 2.0: fast protein–protein docking server. Bioinformatics 32:2386–2388. https://doi.org/10.1093/bioinformatics/btw141
doi: 10.1093/bioinformatics/btw141 pubmed: 27153583
Gabb HA, Jackson RM, Sternberg MJE (1997) Modelling protein docking using shape complementarity, electrostatics and biochemical information 1 1Edited by J. Thornton. J Mol Biol 272:106–120. https://doi.org/10.1006/jmbi.1997.1203
doi: 10.1006/jmbi.1997.1203 pubmed: 9299341
Tovchigrechko A, Vakser IA (2006) GRAMM-X public web server for protein-protein docking. Nucleic Acids Res 34:W310–W314. https://doi.org/10.1093/nar/gkl206
doi: 10.1093/nar/gkl206 pubmed: 16845016 pmcid: 1538913
Yan Y, Zhang D, Zhou P et al (2017) HDOCK: a web server for protein–protein and protein–DNA/RNA docking based on a hybrid strategy. Nucleic Acids Res 45:W365–W373. https://doi.org/10.1093/nar/gkx407
doi: 10.1093/nar/gkx407 pubmed: 28521030 pmcid: 5793843
Macindoe G, Mavridis L, Venkatraman V et al (2010) HexServer: an FFT-based protein docking server powered by graphics processors. Nucleic Acids Res 38:W445–W449. https://doi.org/10.1093/nar/gkq311
doi: 10.1093/nar/gkq311 pubmed: 20444869 pmcid: 2896144
Jiménez-García B, Roel-Touris J, Romero-Durana M et al (2018) LightDock: a new multi-scale approach to protein–protein docking. Bioinformatics 34:49–55. https://doi.org/10.1093/bioinformatics/btx555
doi: 10.1093/bioinformatics/btx555 pubmed: 28968719
Christoffer C, Bharadwaj V, Luu R, Kihara D (2021) LZerD protein-protein docking webserver enhanced with de novo structure prediction. Front Mol Biosci 8. https://doi.org/10.3389/fmolb.2021.724947
Ohue M, Shimoda T, Suzuki S et al (2014) MEGADOCK 4.0: an ultra–high-performance protein–protein docking software for heterogeneous supercomputers. Bioinformatics 30:3281–3283. https://doi.org/10.1093/bioinformatics/btu532
doi: 10.1093/bioinformatics/btu532 pubmed: 25100686 pmcid: 4221127
Berchanski A, Eisenstein M (2003) Construction of molecular assemblies via docking: modeling of tetramers with D2 symmetry. Proteins Struct Funct Genet 53:817–829. https://doi.org/10.1002/prot.10480
doi: 10.1002/prot.10480 pubmed: 14635124
Schneidman-Duhovny D, Inbar Y, Nussinov R, Wolfson HJ (2005) PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res 33:W363–W367. https://doi.org/10.1093/nar/gki481
doi: 10.1093/nar/gki481 pubmed: 15980490 pmcid: 1160241
Kozakov D, Brenke R, Comeau SR, Vajda S (2006) PIPER: an FFT-based protein docking program with pairwise potentials. Proteins Struct Funct Bioinform 65:392–406. https://doi.org/10.1002/prot.21117
doi: 10.1002/prot.21117
Cheng TM-K, Blundell TL, Fernandez-Recio J (2007) pyDock: electrostatics and desolvation for effective scoring of rigid-body protein-protein docking. Proteins Struct Funct Bioinform 68:503–515. https://doi.org/10.1002/prot.21419
doi: 10.1002/prot.21419
Krupa P, Karczyńska AS, Mozolewska MA et al (2021) UNRES-Dock—protein–protein and peptide–protein docking by coarse-grained replica-exchange MD simulations. Bioinformatics 37:1613–1615. https://doi.org/10.1093/bioinformatics/btaa897
doi: 10.1093/bioinformatics/btaa897 pubmed: 33079977
Levieux G, Tiger G, Mader S et al (2014) Udock, the interactive docking entertainment system. Faraday Discuss 169:425–441. https://doi.org/10.1039/C3FD00147D
doi: 10.1039/C3FD00147D pubmed: 25341068
Pierce BG, Wiehe K, Hwang H et al (2014) ZDOCK server: interactive docking prediction of protein-protein complexes and symmetric multimers. Bioinformatics 30:1771–1773. https://doi.org/10.1093/bioinformatics/btu097
doi: 10.1093/bioinformatics/btu097 pubmed: 24532726 pmcid: 4058926

Auteurs

Małgorzata Jarończyk (M)

National Medicines Institute, Warsaw, Poland.

Ruben Abagyan (R)

Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.

Maxim Totrov (M)

Molsoft, LLC, La Jolla, CA, USA.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH