Abstract
Protein–protein docking aims at predicting the three-dimensional structure of a protein complex starting from the free forms of the individual partners. As assessed in the CAPRI community-wide experiment, the most successful docking algorithms combine pure laws of physics with information derived from various experimental or bioinformatics sources. Of these so-called “information-driven” approaches, HADDOCK stands out as one of the most successful representatives. In this chapter, we briefly summarize which experimental information can be used to drive the docking prediction in HADDOCK, and then focus on the docking protocol itself. We discuss and illustrate with a tutorial example a “classical” protein–protein docking prediction, as well as more recent developments for modelling multi-body systems and large conformational changes.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Melquiond AS, Karaca E, Kastritis PL et al (2012) Next challenges in protein–protein docking: from proteome to interactome and beyond. Comput Mol Sci 2:642–651
Kastritis PL, Bonvin AM (2013) Molecular origins of binding affinity: seeking the Archimedean point. Curr Opin Struct Biol 23(6):868–877
Schlick T, Collepardo-Guevara R, Halvorsen LA et al (2011) Biomolecular modeling and simulation: a field coming of age. Quart Rev Biophys 44:191–228
Janin J (2013) The targets of CAPRI rounds 20–27. Proteins 81(12):2075–2081
Lensink MF, Janin J (2013) Docking, scoring and affinity prediction in CAPRI. Proteins 81(12):2082–2095
de Vries SJ, Melquiond ASJ, Kastritis PL et al (2010) Strengths and weaknesses of data-driven docking in critical assessment of prediction of interactions. Proteins 78:3242–3249
Dominguez C, Boelens R, Bonvin AMJJ (2003) HADDOCK: a protein–protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125:1731–1737
Linge JP, Habeck M, Rieping W et al (2003) ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 19:315–316
Brünger AT, Adams PD, Clore GM et al (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905–921
Brunger AT (2007) Version 1.2 of the crystallography and NMR system. Nat Protocol 2:2728–2733
de Vries SJ, Bonvin AMJJ (2008) How proteins get in touch: interface prediction in the study of biomolecular complexes. Curr Protein Pept Sci 9:394–406
Karaca E, Bonvin AMJJ (2013) Advances in integrative modeling of biomolecular complexes. Methods 59:372–381
Schmitz C, Melquiond AS, de Vries SJ et al (2012) Protein–protein docking with HADDOCK, NMR of biomolecules: towards mechanistic systems biology, 1st edn. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, pp 521–535
Wang G, Louis JM, Sondej M et al (2000) Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. EMBO J 19:5635–5649
Bertini I, Calderone V, Cerofolini L et al (2012) The catalytic domain of MMP-1 studied through tagged lanthanides. FEBS Lett 586:557–567
Bax A (2003) Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci 12:1–16
Prestegard JH, Bougault CM, Kishore AI (2004) Residual dipolar couplings in structure determination of biomolecules. Chem Rev 104:3519–3540
Tjandra N (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111–1114
van Dijk ADJ, Fushman D, Bonvin AMJJ (2005) Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data. Proteins 60:367–381
Kalisman N, Adams CM, Levitt M (2012) Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling. Proc Natl Acad Sci U S A 109:2884–2889
Choi UB, Strop P, Vrljic M et al (2010) Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex. Nature 17:318–324
Brunger AT, Strop P, Vrljic M et al (2011) Three-dimensional molecular modeling with single molecule FRET. J Struct Biol 173:497–505
Karaca E, Bonvin AMJJ (2013) On the usefulness of ion-mobility mass spectrometry and SAXS data in scoring docking decoys. Acta Cryst D69:683–694, 1–12
de Vries SJ, Bonvin AMJJ (2011) CPORT: a consensus interface predictor and its performance in prediction-driven docking with HADDOCK. PloS One 6:e17695
Weigt M, White RA, Szurmant H et al (2009) Identification of direct residue contacts in protein–protein interaction by message passing. Proc Natl Acad Sci U S A 106:67–72
Marks DS, Hopf TA, Sander C (2012) Protein structure prediction from sequence variation. Nat Biotechnol 30:1072–1080
Fernández-Recio J, Totrov M, Abagyan R (2004) Identification of protein–protein interaction sites from docking energy landscapes. J Mol Biol 335:843–865
Rodrigues JPGLM, Trellet M, Schmitz C et al (2012) Clustering biomolecular complexes by residue contacts similarity. Proteins 80:1810–1817
Daura X, Gademann K, Jaun B et al (1999) Peptide folding: when simulation meets experiment. Angew Chem Int Ed 38:236–240
Nilges M, O’Donoghue SI (1998) Ambiguous NOEs and automated NOE assignment. Progr Nucl Magn Reson Spectros 32:107–139
Karaca E, Melquiond ASJ, de Vries SJ et al (2010) Building macromolecular assemblies by information-driven docking: introducing the HADDOCK multibody docking server. Mol Cell Proteomics 9:1784–1794
Nilges M (1993) A calculation strategy for the structure determination of symmetric dimers by 1H NMR. Proteins 17:297–309
Schmitz C, Bonvin AMJJ (2011) Protein–protein HADDocking using exclusively pseudocontact shifts. J Biomol NMR 50:263–266
Lee B, Richards FM (1971) The interpretation of protein structures: estimation of static accessibility. J Mol Biol 55:379–400
Karaca E, Bonvin AMJJ (2011) A multidomain flexible docking approach to deal with large conformational changes in the modeling of biomolecular complexes. Structure 19:555–565
van Dijk ADJ, Bonvin AMJJ (2006) Solvated docking: introducing water into the modelling of biomolecular complexes. Bioinformatics 22:2340–2347
Kastritis PL, van Dijk ADJ, Bonvin AMJJ (2012) Explicit treatment of water molecules in data-driven protein–protein docking: the solvated HADDOCKing approach. Methods Mol Biol 819:355–374
Kastritis PL, Visscher KM, van Dijk ADJ et al (2013) Solvated protein–protein docking using Kyte-Doolittle-based water preferences. Proteins 81:510–518
van Dijk M, Visscher KM, Kastritis PL et al (2013) Solvated protein-DNA docking using HADDOCK. J Biomol NMR 56:51–63
Krzeminski M, Loth K, Boelens R et al (2010) SAMPLEX: automatic mapping of perturbed and unperturbed regions of proteins and complexes. BMC Bioinformatics 11:51
Schüttelkopf AW, van Aalten DMF (2004) PRODRG: a tool for high-throughput crystallography of protein–ligand complexes. Acta Crystallogr D Biol Crystallogr 60:1355–1363
Sousa da Silva AW, Vranken WF (2012) ACPYPE – AnteChamber PYthon Parser interfacE. BMC Res Notes 5:367
Malde AK, Zuo L, Breeze M et al (2011) An automated force field topology builder (ATB) and repository: version 1.0. J Chem Theor Comput 7:4026–4037
Lemkul JA, Allen WJ, Bevan DR (2010) Practical considerations for building GROMOS-compatible small-molecule topologies. J Chem Inf Model 50:2221–2235
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer Science+Business Media New York
About this protocol
Cite this protocol
Rodrigues, J.P.G.L.M., Karaca, E., Bonvin, A.M.J.J. (2015). Information-Driven Structural Modelling of Protein–Protein Interactions. In: Kukol, A. (eds) Molecular Modeling of Proteins. Methods in Molecular Biology, vol 1215. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1465-4_18
Download citation
DOI: https://doi.org/10.1007/978-1-4939-1465-4_18
Published:
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-1464-7
Online ISBN: 978-1-4939-1465-4
eBook Packages: Springer Protocols