Abstract
Protein 3-D structural data is a valuable resource in computational biology, and the comparison and interpretation of protein structural patterns have remained scientific and computational challenges. We introduce a novel representation of 3-D protein surface patches as 2-D images, obtained using dimension reduction. We utilize image registration to compare these surface patches and infer protein function and binding based on surface similarity. Our surface representation can capture various structural and physicochemical properties, including curvature, electrostatic potential, hydrophobicity, and evolutionary conservation. The results we present support the use of surface images as a new type of family-specific signatures in functional annotation and drug-binding tasks. We demonstrate the ability of our method to detect local surface similarities between proteins and to correctly identify functional classification of proteins.
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References
Najmanovich, R., Kurbatova, N., Thornton, J.: Detection of 3D atomic similarities and their use in the discrimination of small molecule protein-binding sites. Bioinformatics 24(16), i105–i111 (2008)
Chruszcz, M., et al.: Unmet challenges of structural genomics. Curr. Opin. Struct. Biol. 20(5), 587–597 (2010)
Zhao, C., Sacan, A.: UniAlign: protein structure alignment meets evolution. Bioinformatics 31(19), 3139–3146 (2015)
Sacan, A., et al.: LFM-Pro: a tool for detecting significant local structural sites in proteins. Bioinformatics 23(6), 709–716 (2007)
Hutchinson, E.G., Thornton, J.M.: PROMOTIF–a program to identify and analyze structural motifs in proteins. Protein Sci. 5(2), 212–220 (1996)
Laurie, A.T., Jackson, R.M.: Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites. Bioinformatics 21(9), 1908–1916 (2005)
Hendlich, M., Rippmann, F., Barnickel, G.: LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J. Mol. Graph Model 15(6), 359–363 (1997)
Sael, L., et al.: Rapid comparison of properties on protein surface. Proteins 73(1), 1–10 (2008)
Das, S., Kokardekar, A., Breneman, C.M.: Rapid comparison of protein binding site surfaces with property encoded shape distributions. J. Chem. Inf. Model. 49(12), 2863–2872 (2009)
Kinoshita, K., Nakamura, H.: Identification of protein biochemical functions by similarity search using the molecular surface database eF-site. Protein Sci. 12(8), 1589–1595 (2003)
Connolly, M.L.: The molecular surface package. J. Mol. Graph. 11(2), 139–141 (1993)
Steinkellner, G., et al.: VASCo: computation and visualization of annotated protein surface contacts. BMC Bioinform. 10, 32 (2009)
Fanning, D.W., Smith, J.A., Rose, G.D.: Molecular cartography of globular proteins with application to antigenic sites. Biopolymers 25(5), 863–883 (1986)
Pawlowski, K., Godzik, A.: Surface map comparison: studying function diversity of homologous proteins. J. Mol. Biol. 309(3), 793–806 (2001)
Yang, H., Qureshi, R., Sacan, A.: Protein surface representation and analysis by dimension reduction. Proteome Sci. 10(Suppl. 1), S1 (2012)
Tenenbaum, J.B., de Silva, V., Langford, J.C.: A global geometric framework for nonlinear dimensionality reduction. Science 290(5500), 2319–2323 (2000)
Sheffer, A., Praun, E., Rose, K.: Mesh parameterization methods and their applications. Found. Trends. Comput. Graph. Vis. 2(2), 105–171 (2006)
Levy, B., et al.: Least squares conformal maps for automatic texture atlas generation. In: Proceedings of the 29th Annual Conference on Computer Graphics and Interactive Techniques, pp. 362–371. ACM, San Antonio (2002)
Bertolazzi, P., Guerra, C., Liuzzi, G.: A global optimization algorithm for protein surface alignment. BMC Bioinform. 11, 488 (2010)
Angaran, S., et al.: MolLoc: a web tool for the local structural alignment of molecular surfaces. Nucleic Acids Res. 37(Web Server issue), W565–W570 (2009)
Dong, C.-S., Wang, G.-Z.: Curvatures estimation on triangular mesh. J. Zhejiang Univ. Sci. 6, 128–136 (2005)
Li, L., et al.: DelPhi: a comprehensive suite for DelPhi software and associated resources. BMC Biophys. 5, 9 (2012)
Edgar, R.C.: MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinform. 5, 113 (2004)
Shatsky, M., Nussinov, R., Wolfson, H.J.: Optimization of multiple-sequence alignment based on multiple-structure alignment. Proteins 62(1), 209–217 (2006)
Zhao, W., et al.: Face recognition: a literature survey. ACM Comput. Surv. (CSUR) 35(4), 399–458 (2003)
Bradski, G., Kaehler, A.: Learning OpenCV: Computer Vision with the OpenCV Library. O’reilly, Sebastopol (2008)
Marchitti, S.A., et al.: Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily. Expert Opin. Drug Metab. Toxicol. 4(6), 697–720 (2008)
Porter, C.T., Bartlett, G.J., Thornton, J.M.: The catalytic site atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res. 32(Database issue), D129–D133 (2004)
Huang, B.: MetaPocket: a meta approach to improve protein ligand binding site prediction. OMICS 13(4), 325–330 (2009)
Basu, G., et al.: Electrostatic potential of nucleotide-free protein is sufficient for discrimination between adenine and guanine-specific binding sites. J. Mol. Biol. 342(3), 1053–1066 (2004)
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Yang, H., Zhao, C., Sacan, A. (2017). Unfolding the Protein Surface for Pattern Matching. In: Cai, Z., Daescu, O., Li, M. (eds) Bioinformatics Research and Applications. ISBRA 2017. Lecture Notes in Computer Science(), vol 10330. Springer, Cham. https://doi.org/10.1007/978-3-319-59575-7_8
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DOI: https://doi.org/10.1007/978-3-319-59575-7_8
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