Related ArticlesThree-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Biochemistry. 1993 Jan 26;32(3):754-65
Authors: Meadows RP, Nettesheim DG, Xu RX, Olejniczak ET, Petros AM, Holzman TF, Severin J, Gubbins E, Smith H, Fesik SW
A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been determined using heteronuclear multidimensional nuclear magnetic resonance spectroscopy (NMR) and a distance geometry/simulated annealing protocol. A total of 43 structures of the complex, including 3 tightly bound water molecules, were obtained using 1958 experimental restraints consisting of 1724 nuclear Overhauser effect (NOE) derived distances, 66 chi 1 and 46 phi angular restraints, and 122 hydrogen bond restraints. The root mean square (rms) deviations between the 43 FKBP/ascomycin solution structures and the mean atomic coordinates were 0.43 +/- 0.08 A for the backbone heavy atoms and 0.80 +/- 0.08 A for all non-hydrogen atoms. Angular order parameters for the family of 43 conformations were calculated to determine dihedral convergence. Order parameters for phi, psi, and chi 1 angles exhibited mean values of 0.98, 0.97, and 0.95, respectively, while the mean of the chi 2 order parameter was 0.63. Comparisons were made between the FKBP/ascomycin complex and two NMR-derived solution structures of unbound FKBP and the X-ray crystal structure of an FKBP/FK506 complex. Differences were observed between the FKBP/ascomycin complex and uncomplexed FKBP for residues 33-45 and 78-92. In contrast, the NMR-derived solution structure of the FKBP/ascomycin complex and the X-ray crystal structure of the FKBP/FK506 complex were very similar. Differences between the two complexes were mainly observed in the conformations of some highly solvent exposed side chains.
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
J Magn Reson B. 1994 May;104(1):77-80
Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Biochemistry. 1994 Apr 12;33(14):4093-100
Authors: Cheng JW, Lepre CA, Moore JM
Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
J Magn Reson B. 1994 May;104(1):77-80
Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Biochemistry. 1994 Apr 12;33(14):4093-100
Authors: Cheng JW, Lepre CA, Moore JM
Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc
15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Biochemistry. 1993 Sep 7;32(35):9000-10
Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM
Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppres
Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex.
Related Articles Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex.
Biochemistry. 1993 Mar 16;32(10):2473-80
Authors: Xu RX, Meadows RP, Fesik SW
From a series of 15N-resolved 3D ROESY-HMQC and 13C-resolved 3D NOESY-HMQC spectra of the FK506 binding protein (FKBP)/ascomycin complex in H2O, the locations of three tightly bound water molecules were identified. These waters are all buried within the...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] NMR studies of an FK-506 analog, [U-13C]ascomycin, bound to FK-506-binding protein.
NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein.
Related Articles NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein.
J Med Chem. 1992 Jun 26;35(13):2467-73
Authors: Petros AM, Gemmecker G, Neri P, Olejniczak ET, Nettesheim D, Xu RX, Gubbins EG, Smith H, Fesik SW
Multidimensional, heteronuclear NMR methods were used to determine the complete 1H and 13C resonance assignments for ascomycin bound to recombinant FKBP, including stereospecific assignment of all 22 methylene protons. The...
nmrlearner
Journal club
0
08-21-2010 11:41 PM
[NMR paper] The detection of proline isomerase activity in FK506-binding protein by two-dimension
The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.
Biochem Biophys Res Commun. 1990 Aug 31;171(1):445-50
Authors: Justice RM, Kline AD, Sluka JP, Roeder WD, Rodgers GH, Roehm N, Mynderse JS
1H NMR assignments of the trans and cis isomers of...
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio
Linear Mode
