Steinert M, Hentschel U, Hacker J: Legionella pneumophila : An aquatic microbe goes astray. FEMS Microbiology Reviews 2002, 26: 149–162. 10.1111/j.1574-6976.2002.tb00607.x
Article
CAS
Google Scholar
Köhler R, Fanghänel J, König B, Lüneberg E, Frosch M, Rahfeld J-U, Hilgenfeld R, Fischer G, Hacker J, Steinert M: Biochemical and functional analyses of the Mip protein: Influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila . Infection and Immunity 2004, 71(8):4389–4397. 10.1128/IAI.71.8.4389-4397.2003
Article
Google Scholar
Wagner C, Khan AS, Kamphausen T, Schmausser B, Lorenz U, Fischer G, Hacker J, Steinert M: Collagen binding protein Mip enables Legionella pneumophila to transmigrate through the lung epithelial barrier. Cellular Microbiology 2006, 9: 450–462. 10.1111/j.1462-5822.2006.00802.x
Article
Google Scholar
Schmidt B, Rahfeld J, Schierhorn A, Ludwig B, Hacker J, Fischer G: A homodimer represents an active species of the peptidyl-prolyl cis/trans isomerase FKBP25mem from Legionella pneumophila . FEBS Letters 1994, 352: 185–190. 10.1016/0014-5793(94)00970-8
Article
CAS
Google Scholar
Helbig JH, Lück PC, Steinert M, Jacobs E, Witt M: Immunolocalization of the Mip protein of intracellularly and extracellularly grown Legionella pneumophila . Letters in Applied Microbiology 2001, 32: 83–88. 10.1046/j.1472-765x.2001.00861.x
Article
CAS
Google Scholar
Riboldi-Tunnicliffe A, König B, Jessen S, Weiss MS, Rahfeld J, Hacker J, Fischer G, Hilgenfeld R: Crystal structure of Mip, a prolylisomerase from Legionella pneumophila . Nature Structural Biology 2001, 8: 779–783. 10.1038/nsb0901-779
Article
CAS
Google Scholar
Horstmann M, Ehses P, Schweimer K, Steinert M, Kamphausen T, Fischer G, Hacker J, Rösch P, Faber C: Domain motions of the Mip protein from Legionella pneumophila . Biochemistry 2006, 45: 12303–12311. 10.1021/bi060818i
Article
CAS
Google Scholar
Fischer G, Bang H, Ludwig B, Mann K, Hacker J: Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPIase) activity. Molecular Microbiology 1992, 6: 1375–1383. 10.1111/j.1365-2958.1992.tb00858.x
Article
CAS
Google Scholar
Kino T, Hatanake H, Miyata S, Inamura N, Nishiyama M, Yajima T, Goto T, Okuhara M, Kohsaka M, Aoki H, Ochai T: FK-506, a novel immunosuppressant isolated from a streptomyces. 2. Immunosuppressive effect of FK-506 in vitro. Journal of Antibiotics 1987, 40: 1256–1265.
Article
CAS
Google Scholar
Abraham RT, Wiederrecht GJ: Immunopharmacology of rapamycin. Annual Review of Immunology 1996, 14: 483–510. 10.1146/annurev.immunol.14.1.483
Article
CAS
Google Scholar
Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL: Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991, 66: 807–815. 10.1016/0092-8674(91)90124-H
Article
CAS
Google Scholar
Chen YQ, Chen HH, Rhoad AE, Warner L, Caggiano TJ, Failli A, Zhang HZ, Hsiao CL, Nakanishi K, Molnarkimber KL: A putative Sirolimus (Rapamycin) effector protein. Biochemical and Biophysical Research Communications 1991, 203(1):1–7. 10.1006/bbrc.1994.2140
Article
Google Scholar
Sabatini DM, Erdjument-Bromage H, Lui M, Tempst P, Snyder SH: RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 1991, 78(1):35–43. 10.1016/0092-8674(94)90570-3
Article
Google Scholar
Bierer BE, Mattila PS, Standaert RF, Herzenberg LA, Burakoff SJ, Crabtree G, Schreiber SL: Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed beteen an immunophilin and either FK506 or rapamycin. Proceedings of the National Academy of Sciences 1990, 87: 9231–9235. 10.1073/pnas.87.23.9231
Article
CAS
Google Scholar
Leuzzi R, Serino L, Scarselli M, Savino S, Fontana MR, Monaci E, Taddei A, Fischer G, Rappuoli R, Pizza M: Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Molecular Microbiology 2005, 58: 669–681. 10.1111/j.1365-2958.2005.04859.x
Article
CAS
Google Scholar
Lundemose AG, Birkelund S, Fey SJ, Larsen PM, Christiansen G: Chlamydia trachomatis contains a protein similar to the Legionella pneumophila mip gene product. Molecular Microbiology 1991, 5: 109–115. 10.1111/j.1365-2958.1991.tb01831.x
Article
CAS
Google Scholar
Moro A, Ruiz-Cabello F, Fernández-Cano A, Stock RP, González A: Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection. Embo Journal 1995, 14: 2483–2490.
CAS
Google Scholar
Bell A, Monaghan P, Page AP: Peptidyl-prolyl cis-trans isomerases (immunophilins) and their roles in parasite biochemistry, host-parasite interaction and antiparasitic drug action. International Journal for Parasitology 2006, 36: 261–276. 10.1016/j.ijpara.2005.11.003
Article
CAS
Google Scholar
Engleberg NC, Carter C, Weber DR, Cianciotto NP, Eisenstein BI: DNA sequence of Mip, a Legionella pneumophila gene associated with macrophage infectivity. Infection and Immunity 1989, 574: 1263–1270.
Google Scholar
Tjandra N, Kuboniwa H, Ren H, Bax A: Rotational-dynamics of calcium-free calmodulin studied by N-15-NMR relaxation measurements. European Journal of Biochemistry 1995, 230: 1014–1024. 10.1111/j.1432-1033.1995.tb20650.x
Article
CAS
Google Scholar
De la Torre JG, Huertas ML, Carrasco B: HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. Journal of Magnetic Resonance 2000, 147: 138–146. 10.1006/jmre.2000.2170
Article
Google Scholar
Wintermeyer E, Ludwig B, Steinert M, Schmidt B, Fischer G, Hacker J: Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infection and Immunity 1995, 63(12):4576–4583.
CAS
Google Scholar
Galat A: Sequence diversification of the FK506-binding proteins in several different genomes. European Journal of Biochemistry 2000, 267: 4945–4959. 10.1046/j.1432-1327.2000.01509.x
Article
CAS
Google Scholar
DePristo MA, Weinreich DM, Hartl DL: Missense meanderings in sequence space: A biophysical view of protein evolution. Nature Reviews Genetics 2005, 6: 678–687. 10.1038/nrg1672
Article
CAS
Google Scholar
Wilson KP, Yamashita MM, Sintchak MD, Rotstein SH, Murcko MA, Boger J, Thomson JA, Fitzgibbon MJ, Black JR, Navia MA: Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin. Acta Crystallographica Section D Biological Crystallography 1995, 51(4):511–521. 10.1107/S0907444994014514
Article
CAS
Google Scholar
Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL: Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science 1991, 252: 836–839. 10.1126/science.1709301
Article
CAS
Google Scholar
Van Duyne GD, Standaert RF, Schreiber SL, Clardy J: Atomic structure of the rapamycin human immunophilin FKBP-12 complex. Journal of the American Chemical Society 1991, 113: 7433–7434. 10.1021/ja00019a057
Article
CAS
Google Scholar
Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J: Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. Journal of Molecular Biology 1993, 229: 105–124. 10.1006/jmbi.1993.1012
Article
CAS
Google Scholar
Cheng J-W, Lepre CA, Moore JM: 15N NMR relaxation studies of the FK506 binding protein: Dynamic effects of ligand binding and implications for Calcineurin recognition. Biochemistry 1994, 33: 4093–4100. 10.1021/bi00180a001
Article
CAS
Google Scholar
Bossard MJ, Bergsma DJ, Brandt M, Livi GP, Eng W-K, Johnson RK, Levy MA: Catalytic and ligand binding properties of the FK506 binding protein FKBP12: effects of the single amino acid substitution of Tyr82to Leu. Biochemical Journal 1994, 297: 365–372.
Article
CAS
Google Scholar
Park ST, Aldape RA, Futer O, Decenzo MT, Livingston DJ: PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. Journal of Biological Chemistry 1992, 267: 3316–3324.
CAS
Google Scholar
Fretz H, Albers MW, Galat A, Standaert RF, Lane WS, Burakoff SJ, Bierer BE, Schreiber SL: Rapamycin and FK506 binding proteins (immunophilins). Journal of the American Chemical Society 1991, 113: 1409–1411. 10.1021/ja00004a051
Article
CAS
Google Scholar
Armistead DM, Badia MC, Deininger DD, Duffy JP, Saunders JO, Tung RD, Thomsin JA, Decenzo MT, Futer O, Livingston DJ, Murcko MA, Yamashita MM, Navia MA: Design, synthesis and structure of non-macrocyclic inhibitors of FKBP12, the major binding protein for the immunosuppressant FK506. Acta Crystallographica Section D Biological Crystallography 1995, 51(4):522–528. 10.1107/S0907444994014502
Article
CAS
Google Scholar
Babine RE, Bleckman TM, Littlefield ES, Parge HE, Pelletier LAK, Lewis CT, French JV, Imbacuan M, Katoh S, Tatlock JH, Showalter RE, Ernest J: Design, synthesis and X-ray crystallographic studies of [7.3.1] and [8.3.1] macrocyclic FKBP-12 ligands. Bioorganic & Medicinal Chemistry Letters 1996, 6: 385–390. 10.1016/0960-894X(96)00032-7
Article
CAS
Google Scholar
Wang XJ, Etzkorn FA: Peptidyl-prolyl isomerase inhibitors. Biopolymers 2006, 84: 125–146. 10.1002/bip.20240
Article
CAS
Google Scholar
Gold BG, Zeleny-Pooley M, Wang M-S, Chaturvedi P, Armistead DM: A nonimmunosuppressant FKBP-12 ligand increases nerve regeneration. Experimental Neurology 1997, 147: 269–278. 10.1006/exnr.1997.6630
Article
CAS
Google Scholar
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A: NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Journal of Biomolecular NMR 1995, 6: 277–293. 10.1007/BF00197809
Article
CAS
Google Scholar
Horstmann M, Kamphausen T, Schweimer K, Steinert M, Hacker J, Haase A, Rösch P, Fischer G, Faber C: 1H, 13C, 15N backbone and side chain resonance assignment of Mip(77–213)the PPIase domain of the Legionella pneumophila Mip protein. Journal of Biomolecular NMR 2005, 31: 77–78. 10.1007/s10858-004-6041-6
Article
CAS
Google Scholar
Johnson BA, Blevins RA: NMR View: A computer program for the visualization and analysis of NMR data. Journal of Biomolecular NMR 1994, 4: 603–614. 10.1007/BF00404272
Article
CAS
Google Scholar
Dayie KT, Wagner G: Relaxation-rate measurements for N-15-H-1 groups with pulsed-field gradients and preservation of coherence pathways. Journal of Magnetic Resonance Series A 1994, 111: 121–126. 10.1006/jmra.1994.1236
Article
CAS
Google Scholar
Markus MA, Dayie KT, Matsudaira P, Wagner G: Effect of deuteration on the amide proton relaxation rates in proteins: heteronuclear NMR experiments on villin 14T. Journal of Magnetic Resonance Series B 1994, 105: 192–195. 10.1006/jmrb.1994.1122
Article
CAS
Google Scholar
Blackledge M, Cordier F, Dosset P, Marion D: Precision and uncertainty in the characterization of anisotropic rotational diffusion by N-15 relaxation. Journal of the American Chemical Society 1998, 120: 4538–4539. 10.1021/ja9742646
Article
CAS
Google Scholar
Dosset P, Hus JC, Blackledge M, Marion D: Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. Journal of Biomolecular NMR 2000, 16: 23–28. 10.1023/A:1008305808620
Article
CAS
Google Scholar
Linge JP, Habeck M, Rieping W, Nilges M: ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 2003, 19: 315–316. 10.1093/bioinformatics/19.2.315
Article
CAS
Google Scholar
Brunger AT, Adams PD, Clore GM, Delano WL, Gros P, Grosse-Kunstleve RW, Jiang J-S, Kuszewskim J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL: Crystallography & NMR system: A new software suit for macromolecular structure determination. Acta Crystallographica Section D Biological Crystallography 1998, 54(5):905–921. 10.1107/S0907444998003254
Article
CAS
Google Scholar
Cornilescu G, Delaglio F, Bax A: Protein backbone angle restraints from searching a database for chemical shift and sequence homology. Journal of Biomolecular NMR 1999, 13: 289–302. 10.1023/A:1008392405740
Article
CAS
Google Scholar
Schwieters CD, Kuszewski JJ, Tjandra N, Clore GM: The Xplor-NIH NMR molecular structure determination package. Journal of Magnetic Resonance 2003, 160: 65–73. 10.1016/S1090-7807(02)00014-9
Article
CAS
Google Scholar
Schwieters CD, Kuszewski JJ, Clore GM: Using Xplor-NIH for NMR molecular structure determination. Progress in Nuclear Magnetic Resonance Spectroscopy 2006, 48: 47–62. 10.1016/j.pnmrs.2005.10.001
Article
CAS
Google Scholar
Schuettelkopf AW, van Aalten DMF: PRODRG – a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallographica Section D Biological Crystallography 2004, 60: 1355–1363. 10.1107/S0907444904011679
Article
Google Scholar
Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J: Interaction models for water in relation to protein hydration. Dordrecht, The Netherlands, D. Reider Publishing Co; 1981.
Book
Google Scholar
Berendsen HJC, van der Spoel D, van Drunen R: Gromacs – a message-passing parallel molecular-dynamics implementation. Computer Physics Communications 1995, 91: 43–56. 10.1016/0010-4655(95)00042-E
Article
CAS
Google Scholar
Lindahl E, Hess B, van der Spoel D: GROMACS 3.0: a package for molecular simulation and trajectory analysis. Journal of Molecular Modeling 2001, 7: 306–317.
CAS
Google Scholar
Van der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJC: GROMACS: Fast, flexible, and free. Journal of Computational Chemistry 2005, 26: 1701–1718. 10.1002/jcc.20291
Article
CAS
Google Scholar
DeLano WL: The PyMOL molecular graphics system. San Carlos, CA, USA, DeLano Scientific; 2002.
Google Scholar
Laskowski R, MacArthur M, Moss D, Thornton J: PROCHECK: a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography 1993, 26: 283–291. 10.1107/S0021889892009944
Article
CAS
Google Scholar
Chenna R, Sugawara H, Koike T, Lopez R, Gibson TJ, Higgins DG, Thompson JD: Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Research 2003, 31: 3497–3500. 10.1093/nar/gkg500
Article
CAS
Google Scholar
Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG: The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Research 1997, 24: 4876–4882. 10.1093/nar/25.24.4876
Article
Google Scholar
Worldwide protein data bank[http://www.wwpdb.org]