Related Articles15N 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 1H-15N NMR spectra. A model free formalism [Lipari & Szabo (1982) J. Am. Chem. Soc. 104, 4546-4559] was used to derive the generalized order parameter (S2), the effective correlation time for internal motions (tau e), and the chemical-exchange line width (R(ex)) based on the measured 15N relaxation rate constants (R1, R2) and 1H-15N heteronuclear NOEs. The final optimized overall correlation time (tau m) was 9.0 ns. The average order parameter (S2) describing the amplitude of motions on the picosecond time scale was found to be 0.88 +/- 0.04, indicating that internal flexibility is restricted along the entire polypeptide chain. In contrast to results obtained for uncomplexed FKBP, the 80's loop (residues 82-87) surrounding the ligand binding site was found to be rigidly fixed, indicating that internal motions at this site are damped significantly due to stabilizing noncovalent interactions with the FK506 molecule. Structural implications of these differences in picosecond mobility as well as possible implications for calcineurin recognition are discussed.
[NMR paper] Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly
Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin fragment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin...
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[NMR paper] NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies
NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
Biochemistry. 1996 Jul 30;35(30):9637-46
Authors: Scheuring J, Fischer M, Cushman M, Lee J, Bacher A,...
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[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
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[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...
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Journal club
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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
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[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....
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[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...
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[NMR paper] Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Related Articles Three-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...
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
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