Abstract
Protein dimers are common in catalysis and regulation. Their associations are either homodimers (identical monomers) or heterodimers (nonidentical monomers). The molecular principles of protein dimer interactions are difficult to understand mainly due to the geometrical and chemical characteristics of proteins. Nonetheless, the principles of protein dimer interactions are often studied using a dataset of 3D structural complexes determined by X-ray crystallography. A number of physical and chemical properties govern protein dimer interactions. Yet, a handful of such properties are known to dominate protein dimer interfaces. The principles of protein-protein interactions (PPI) are discussed.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Bahadur RP, Chakrabarti P, Rodier F et al (2003) Dissecting subunit interfaces in homodimeric proteins. Proteins 53:708–719
Brinda KV, Kannan N, Vishveshwara S (2002) Analysis of homodimeric protein interfaces by graph-spectral methods. Protein Eng 15:265–277
Caffrey DR, Somaroo S, Hughes JD et al (2004) Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 13:190–202
Chakrabarti P, Janin J (2002) Dissecting protein-protein recognition sites. Proteins 47:334–343
Dasgupta S, Iyer GH, Bryant SH et al (1997) Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins 28:494–514
Jones S, Thornton JM (1995) Protein-protein interactions: a review of protein dimer structures. Prog Biophys Mol Biol 63:31–65
Jones S, Thornton JM (1996) Principles of protein-protein interactions. Proc Natl Acad Sci U S A 93:13–20
Kangueane P, Nilofer C (2018) Protein–protein and domain–domain interactions. Springer Nature, p 1–207. ISBN: 978-981-10-7346-5
Lijnzaad P, Argos P (1997) Hydrophobic patches on protein subunit interfaces: characteristics and prediction. Proteins 28:333–343
Li L, Zhao B, Cui Z, Gan J, Sakharkar M, Kangueane P (2006) Identification of hot spot residues at protein-protein interface. Bioinformation 1(4):121–126
Lo Conte L, Chothia C, Janin J (1999) The atomic structure of protein-protein recognition sites. J Mol Biol 285:2177–2198
Nilofer C, Sukhwal A, Mohanapriya A, Kangueane P (2017) Protein-protein interfaces are vdW dominant with selective H-bonds and (or) electrostatics towards broad functional specificity. Bioinformation 13(6):164–173
Nooren IM, Thornton JM (2003) Structural characterisation and functional significance of transient protein-protein interactions. J Mol Biol 325:991–1018
Sowmya G, Anita S, Kangueane P (2011) Insights from the structural analysis of protein heterodimer interfaces. Bioinformation 6:137–143
Tsai CJ, Lin SL, Wolfson HJ et al (1997) Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci 6:53–64
Valdar WS, Thornton JM (2001) Conservation helps to identify biologically relevant crystal contacts. J Mol Biol 313:399–416
Xu D, Tsai CJ, Nussinov R (1997) Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 10:999–1012
Zhanhua C, Gan JG, Lei L et al (2005) Identification of critical heterodimer protein interface parameters by multi-dimensional scaling in Euclidian space. Front Biosci 10:844–852
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG, part of Springer Nature
About this chapter
Cite this chapter
Kangueane, P. (2018). Protein-Protein Interaction. In: Bioinformation Discovery. Springer, Cham. https://doi.org/10.1007/978-3-319-95327-4_4
Download citation
DOI: https://doi.org/10.1007/978-3-319-95327-4_4
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-95326-7
Online ISBN: 978-3-319-95327-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)