Keywords: Chemical Bonds, Computer Simulation, Diseases, Molecular Dynamics, Molecular Structure, Nuclear Magnetic Resonance Spectroscopy, Proteins, X Ray Crystallography, Angiostatin, Plasminogen, Prion Protein, Molecular Biology,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Univ. Studi di Modena Reggio Emilia, Via Campi 183, 41100 Modena, Italy
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Novokhatny, V. V., Kudinov, S. A., Privalov, P., (1984) J. Molec. Biol., 179, p. 215
Rios-Steiner, J. L., Schenone, M., Mochalkin, I., Tulinsky, A., Castellano, F. J., (2001) J. Molec. Biol., 308, p. 705
Mulichak, A. M., Tulinsky, A., Ravichandran, K. G., (1991) Biochemistry, 30, p. 10576
Mathews, I. I., Vanderhoff-Hanaver, P., Castellino, F. J., Tulinsky, A., (1996) Biochemistry, 35, p. 2567
Abad, M. C., Arni, R. K., Grella, D. K., Castellino, F. J., Tulinsky, A., Geiger, J. H., (2002) J. Mol. Biol., 318, p. 1009
Marti, D. N., Hu, C. -K., An, S. S. A., Von Haller, P., Schaller, J., Llinas, M., (1997) Biochemistry, 36, p. 11591
Wu, T. P., Padmanabhan, K., Tulinsky, A., Mulichak, A. M., (1991) Biochemistry, 30, p. 10589
McCance, S. G., Menhart, N., Castellino, F. J., (1994) J. Biol. Chem., 269, p. 32405
Graversen, J. H., Sigurskjold, B. W., Thogersen, H. C., Etzerodt, M., (2000) Biochemistry, 39, p. 7414
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., Karplus, M., (1983) J. Comput. Chem., 4, p. 187
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Jorgensen, W. L., Tirado-Rives, J., (1988) J. Am. Chem. Soc., 110, p. 1657
Devis, M. E., McCammon, J. A., (1991) J. Comput. Chem., 12, p. 909
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Seeking for binding determinants of the prion protein to human plasminogen
Plasminogen (Pg), a pro-protease implicated in neuronal excitotoxicity, has recently been identified as binding to prion protein (PrP) from several species. Although the precise effect of the binding of PrP to plasminogen in the course of prion-caused diseases has not yet been demonstrated, the implications of this important finding for diagnostic applications are straightforward. In this paper we have investigated the possible modes of interaction of PrP with plasminogen, by means of molecular modelling and computational simulation techniques. To this goal, we first exploited the information available for the mK2Pg/VEK-30 complex in order to identify the PrP residues which satisfy the specific electronic and geometric requirements needed to interact with the kringle lysine binding site, we compared the relevant mK2Pg/VEK-30 and mK2Pg/PrP interactions obtained from the simulated protein-protein complexes and we assessed the docking hypothesis utilized for the mK2Pg/PrP complex by simulating the interaction of PrP with the multi-kringle angiostatin, a more realistic model of the physiological target. The results obtained will be instrumental for planning experiments tailored to clarify the role of the plasminogen activator system in prion-related diseases and, eventually, for mimicking dominant binding determinants through structure-based drug design.
Seeking for binding determinants of the prion protein to human plasminogen
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(360 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote