Related ArticlesNMR studies of an FK-506 analog, [U-13C]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 [U-13C]ascomycin bound to recombinant FKBP, including stereospecific assignment of all 22 methylene protons. The conformation of ascomycin was then determined from an analysis of NOEs observed in a 13C-edited 3D HMQC-NOESY spectrum of the [U-13C]ascomycin/FKBP. This structure is found to be quite different from the solution structure of the two forms of uncomplexed FK-506. However, it is very similar to the X-ray crystal structure of FK-506 bound to FKBP, rms deviation = 0.56 A. The methods used for resonance assignment and structure calculation are presented in detail. Furthermore, FKBP/ascomycin NOEs are reported which help define the structure of the ascomycin binding pocket. This structural information obtained in solution was compared to the recently described X-ray crystal structure of the FKBP/FK-506 complex.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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[NMR paper] NMR studies of the phosphorylation motif of the HIV-1 protein Vpu bound to the F-box
NMR studies of the phosphorylation motif of the HIV-1 protein Vpu bound to the F-box protein beta-TrCP.
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Biochemistry. 2003 Dec 23;42(50):14741-51
Authors: Coadou G, Gharbi-Benarous J, Megy S, Bertho G, Evrard-Todeschi N, Segeral E, Benarous R, Girault JP
A protein-protein association regulated by phosphorylation of serine is examined by NMR studies. Degradation of the HIV receptor CD4 by the proteasome, mediated by the HIV-1...
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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] 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] 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.
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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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08-21-2010 11:53 PM
[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...
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[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
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Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
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08-21-2010 11:12 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
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NMR studies of an FK-506 analog, [U-13C]ascomycin, bound to FK-506-binding protein.
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