Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja0570279
Title: Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy
Authors: Brath, U.
Akke, M.
Yang, D. 
Kay, L.E.
Mulder, F.A.A.
Issue Date: 3-May-2006
Citation: Brath, U., Akke, M., Yang, D., Kay, L.E., Mulder, F.A.A. (2006-05-03). Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society 128 (17) : 5718-5727. ScholarBank@NUS Repository. https://doi.org/10.1021/ja0570279
Abstract: Transverse relaxation dispersion NMR spectroscopy can provide atom-specific information about time scales, populations, and the extent of structural reorganization in proteins under equilibrium conditions. A method is described that uses side-chain methyl groups as local reporters for conformational transitions taking place in the microsecond regime. The experiment measures carbon nuclear spin relaxation rates in the presence of continuous wave off-resonance irradiation, in proteins uniformly enriched with 13C, and partially randomly labeled with 2H. The method was applied to human FK-506 binding protein (FKBP12), which uses a common surface for binding substrates in its dual role as both an immunophilin and folding assistant. Conformational dynamics on a time scale of ∼130 μs were detected for methyl groups located in the substrate binding pocket, demonstrating its plasticity in the absence of substrate. The spatial arrangement of affected side-chain atoms suggests that substrate recognition involves the rapid relative movement of the subdomain comprising residues Ala81-Thr96 and that the observed dynamics play an important role in facilitating the interaction of this protein with its many partners, including calcineurin. © 2006 American Chemical Society.
Source Title: Journal of the American Chemical Society
URI: http://scholarbank.nus.edu.sg/handle/10635/100722
ISSN: 00027863
DOI: 10.1021/ja0570279
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

51
checked on May 7, 2021

WEB OF SCIENCETM
Citations

52
checked on May 7, 2021

Page view(s)

55
checked on May 2, 2021

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.