NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax
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Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Feske S, Okamura H, Hogan PG, Rao A (2003) Ca2+/calcineurin signaling in cells of the immune system. Biochem Biophys Res Commun 311:1117–1132
Galat A (2003) Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr Top Med Chem 3:1315–1347
Gothel SF, Marahiel MA (1999) Peptidyl-prolyl cis–trans isomerase, a superfamily of ubiquitin folding catalyst. Cell Mol Life Sci 55:423–436
Kang CB, Tai J, Chia J, Yoon HS (2005) The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38). FEBS Lett 579:1469–1476
Kang CB, Ye H, Yoon HR, Yoon HS (2008) Solution structure of FK506 binding domain (FKBD) of Plasmodium falciparum FK506 binding protein 35 (PfFKBP35). Proteins 70:300–302
Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, Gastinel LN, Habuka N, Chen X, Maldonado F, Barker JE, Bacquet R, Villafranca JE (1995) Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex. Nature 378:641–644
Kumar R, Adams B, Musiyenko A, Shulyayeva O, Barik S (2005) The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. Mol Biochem Parasitol 141:163–173
Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL (1991) Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science 252:836–839
Monaghan P, Bell A (2005) A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl–prolyl cis–trans isomerase and chaperone activities. Mol Biochem Parasitol 139:185–195
Ratajczak T, Ward BK, Minchin RF (2003) Immunophilin chaperones in steroid receptor signalling. Curr Top Med Chem 3:1348–1357
Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF (2004) Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit Rev Biochem Mol Biol 39:279–295
Satller M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spectrosc 34:93–158
World Health Organisation (2005) World Malaria Report