National Tsing Hua University Institutional Repository:15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcineurin Recognition
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    NTHUR > College of Life Sciences  > Life Sciences > LIFE Journal / Magazine Articles  >  15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcineurin Recognition


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/49291


    Title: 15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcineurin Recognition
    Authors: Jya-Wei Cheng;Christopher A. Lepre;Jonathan M. Moore
    Teacher: 程家維
    Date: 1994
    Publisher: American Chemical Society
    Relation: BIOCHEMISTRY,American Chemical Society,Volume 33,Issue 14,APR 12 1994,Pages 4093-4100
    Keywords: MAGNETIC-RESONANCE RELAXATION
    MODEL-FREE APPROACH
    Abstract: Backbone dynamics of the ligand- (FK506-) bound protein FKBP- 12 (107 amino acids) have been examined using N-15 relaxation data derived from inverse-detected two-dimensional H-1-N-15 NMR spectra. A model free formalism [Lipari & Szabo (1982) J. Am. Chem. Soc. 104, 4546-45591 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 H-1-N-15 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.
    URI: http://pubs.acs.org/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/49291
    Appears in Collections:[ Life Sciences] LIFE Journal / Magazine Articles

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