Abstract
How vital cellular processes are exquisitely coupled at the molecular level to properly regulate cell division, growth and proliferation is one of the major issues in biological research. This coupling involves the transduction of extracellular signals via membrane proteins to control an entire cascade of biochemical events in the cell. A key element of signaling cascades is the control of protein-protein association through phosphorylation of tyrosine residues.
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References
Balaram, P., Bothney-By, A.A. and Breslow, E., 1973, “nuclear Magnetic Resonance Studies of the Interaction of Peptides and Hormones with Bovine Neurophysin,” Biochemistry 12:4695.
Boivin, P. and Galand, C., 1986, “The Human Red Cell Acid Phosphatase is a Phosphotyrosine Protein Phosphatase which Dephosphorylates the Membrane Protein Band 3,” Biochem. Biophys. Res. Com. 134:557.
Brünger, A.T., 1993,X-PLOR 3.1 Manual, Yale University, New Haven,CT.
Campbell, A.P. and Sykes, B.D., 1991, “Theoretical Evaluation of the Two-Dimensional Transferred Nuclear Overhauser Effect,” J. Magn. Reson. 93:77.
Clore, G.M. and Gronenborn, A.M., 1982, “Theory and Applications of the Transferred Nuclear Overhauser Effect to Determine the Structure of the Inhibitory Troponin I Peptide when Bound to Skeletal Troponin C,” J. Mol. Biol. 48:402.
Clore, G.M. and Gronenborn, A.M., 1983, “Theory of the Time Dependent Transferred Nuclear Overhauser Effect: Applications to Structural Analysis of Ligand-Protein Complexes in Solution,” J. Mag. Res. 53:423.
Harrison, M.L., Isaacson, C.C., Burg, D.L., Geahlen, R.L. and Low, P.S., 1994, “Phosphorylation of Human Erythrocyte Band 3 by Endogenous p72syk,” J. Biol. Chem. 269:955.
Harrison, M.L., Rathinavelu, P., Arese, P., Geahlen, R.L. and Low, P.S., 1991, “Role of Band 3 Tyrosine Phosphorylation in the Regulation of Erythrocyte Glycolysis,” J. Biol. Chem. 266:4106.
Karpen, M.E., Tobias, D.J. and Brooks, C.L., III, 1993, “Statistical Clustering Techniques for the Analysis of Long Molecular Dynamics Trajectories: Analysis of 2.2-ns Trajectories of YPGDV,” Biochemistry 32:412.
Landy, S.B. and Rao, B.D.N., 1989, “Dynamical NOE in Multiple Spin Systems Undergoing Chemical Exchange,” J. Magn. Reson. 81:371.
London, R.E., Perlman, M.E. and Davis, D.G., 1992, “Relaxation-Matrix Analysis of the Transferred Nuclear Overhauser Effect for Finite Exchange Rates,” J. Magn. Reson. 97:79.
Low, Philip S., 1986, “Structure and Function of the Cytoplasmic Domain of Band 3: Center of Erythrocyte Membrane-peripheral Protein Interactions,” Biochimica et Biophysica Acta 864:145.
Low, P.S., Allen, D.P., Zioncheck, T.F., Chari, P., Willardson, B.M., Geahlen, R.L., and Harrison, M.L., 1987, “Tyrosine Phosphorylation of Band 3 Inhibits Peripheral Protein Binding,” J. Biol. Chem. 262:4592.
Low, P.S., Rathinavelu, P. and Harrison, M.L., 1993, “Regulation of Glycolysis via Reversible Enzyme Binding to the Membrane Protein, Band 3,” J. Biol. Chem. 268:14267.
Ni, F., 1992, “Complete Relaxation Matrix Analysis of Transferred Nuclear Overhauser Effects,” J. Magn. Reson. 96:651.
Ni, F. and Zhu, Y., 1994, “Accounting for Ligand-Protein Interactions in the Relaxation Matrix Analysis of Transferred Nuclear Overhauser Effects,” J. Magn. Reson. 103:180.
Post, C.B., Meadows, R.P. and Gorenstein, D.G., 1990, “On the Evaluation of Interproton Distances for Three-Dimensional Structure Determination by NMR Using a Relaxation Rate Matrix Analysis,” J. Am. Chem. Soc. 112:6796.
Prasanna Murthy, S.M., Liu, Theresa, Kaul, R.K., Kohler, H. and Steck, T.L., 1981, “The Aldolase-binding Site of the Human Erythrocyte Membrane is at the NH2 Terminus of Band 3,” J. Biol. Chem. 256:11203.
Salhany, J.M., 1990, “Erythrocyte Band 3 Protein,” CRC Press, Inc., Boca Raton,FL. Schneider, M.L. and Post, C.B., 1995, “Structure of a Phospho-tyrosyl Band 3 Peptide When Bound to Aldolase from Exchange-Transferred Nuclear Overhauser NMR,” submitted.
Stanfield, R.I. and Wilson, I.A., 1995, “Protein-Peptide Interactions,” Curr. Opin. Struct. Biol. 5:103.
Sygusch, J., Beaudry, D. and Allaire, M., 1987, “Molecular Architecture of Rabbit Skeletal Muscle Aldolase at 2.7-A Resolution,” Proc. Natl. Acad. Sci. USA 84:7846.
van Schaik, R.C., Berendsen, H.J.C., Torda, A.E. and van Gunsteren, W.F., 1993, “A Structure Refinement Method Based on Molecular Dynamics in Four Spatial Dimensions,” J. Mol. Biol. 234:751.
Waksman, G., Kominos, D., Robertson, S.C., Pant, N., Baltimore, D., Birge, R.B., Cowburn, D., Hanafusa, H., Mayer, B.J., Overduin, M., Resh, M.D., Rios, C.B., Silverman, L. and Kuriyan, J., 1992, “Crystal Structure of the Phosphotyrosine Recognition Domain SH2 of v-src Complexed with Tyrosine-phosphorylated Peptides,” Science 358:646
Xu, R.X., Word, M., Davis, D.G., Rink, M.J., Willard, D.H. Jr. and Gampe, R.T. Jr., 1995, “Solution Structure of the Human pp60c-scr SH2 Domain Complexed with a Phosphorylated Tyrosine Pentapeptide,” Biochemistry 34:2107.
Zheng, J and Post, C.B., 1993, “Protein Indirect Relaxation Effects in Exchange- Transferred NOESY by a Rate-Matrix Analysis,” J. Magn. Res. 101:262.
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Thomas James - Carol, with the final six model structures that you got which have a lot of similarity, you should be able to use your protein-ligand interactions, go back through your relaxation matrix calculations, maybe even come up with a new set of distances, perhaps even do structure calculations beyond that. Of course, if you went back through that, it should be entirely consistent with the models as you presented them. Have you done this sort of thing?
Carol Post - No, we haven’t done that. We have just obtained the complexes. It is certainly the direction we’re heading. The difficulty is that we know there is heterogeneity because of the titration. We know that the various amide regions have different effective correlation times, so they’re either heterogeneous in conformation or they’re literally bound less tightly and have faster correlation times. So, to really go back and reproduce the data will be difficult. I am somewhat worried that we do not have enough data to really distinguish all the possibilities. It is the usual thing that if you have enough parameters, you’ll fit everything. I think it is quite clear though that the loop region is as we’ve defined it.
Thomas Hurley - I was just curious; in the molecular dynamics simulation, how is the structure of the enzyme treated during the simulation?
Post - For the complex?
Hurley - Yes.
Post - Michael fixed the region which is distant to the peptide and allowed only the region o
within about 15 Å or so of the peptide to move. Again, it was just an idea of trying to “jiggle” the system up a bit to get a better interaction, and the interactions turned out to be very nice actually. The interaction energies between the peptide and the protein are very low.
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© 1996 Plenum Press, New York
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Post, C.B., Schneider, M.L. (1996). Phosphotyrosyl Peptide-Enzyme Complexes: How Much Structure Can We Get From Transferred Noe’s. In: Rao, B.D.N., Kemple, M.D. (eds) NMR as a Structural Tool for Macromolecules. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0387-9_7
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DOI: https://doi.org/10.1007/978-1-4613-0387-9_7
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