The structural modeling of EF-hand motifs in parvalbumin
- 1 Downloads
Parvalbumin (Parv) is a typical protein with EF-hand motifs that play an important role in many physiological processes. We present a novel free energy to model the skeletal C\(_\alpha \) chain of the protein from the basic principle of mathematics and physics. Starting from the crystal structure of Parv (PDB code 2PVB), we first analyze the profile of the C\(_\alpha \) bond and torsion angles over the segment that contains the secondary structures. Then the parameters in the energy function are evaluated for the helix ABCD fragment that contains two EF-hand domains in Parv. Meanwhile an eight-soliton configuration at the energy minimum is constructed to model the conformation of ABCD fragment. The deviation of the conformation constructed from the model away from the crystal structure is as small as 1.28 Å. The structural modeling stems from the physical energy, which is a benefit relative to the statistics-based or knowledge-based technologies.
KeywordsParvalbumin EF-hand Protein structural modeling Free energy Soliton
We would like to thank Prof. Antti J. Niemi of Uppsala University, our cooperator in biophysics, for continued discussions on the theory and method. We also thanks the support of the international cooperation project of Beijing Institute of Technology.
- 3.H. Kawasaki, R.H. Kretsinger, Calcium-binding proteins 1: EF-hands. Protein Profile 1, 343–517 (1994)Google Scholar
- 7.R.H. Kretsinger, C.E. Nockolds, Carp muscle calcium-binding protein. J. Biol. Chem. 248, 3313–3326 (1973)Google Scholar
- 27.I. Sillitoe, T.E. Lewis, A. Cuff, S. Das, P. Ashford, N.L. Dawson, N. Furnham, R.A. Laskowski, D. Lee, J.G. Lees, S. Lehtinen, R.A. Studer, J. Thornton, C.A. Orengo, CATH: comprehensive structural and functional annotations for genome sequences. Nucleic Acids Res. 43(D1), D376–D381 (2015)CrossRefGoogle Scholar
- 28.A.G. Murzin, S.E. Brenner, T. Hubbard, C. Chothia, SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536–540 (1995)Google Scholar