NMR 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. doi: 10.1021/jm00091a015.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Line
  • Escherichia coli / genetics
  • Gene Expression
  • Genes, Bacterial
  • Humans
  • Magnetic Resonance Spectroscopy
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • T-Lymphocytes / metabolism
  • Tacrolimus / analogs & derivatives*
  • Tacrolimus / chemistry
  • Tacrolimus / metabolism
  • Tacrolimus Binding Proteins
  • X-Ray Diffraction

Substances

  • Carbon Isotopes
  • Carrier Proteins
  • Recombinant Proteins
  • immunomycin
  • Tacrolimus Binding Proteins
  • Tacrolimus