Download MendeleySolution structures of human transforming growth factor alpha derived from 1H NMR data.
Kline, T.P., Brown, F.K., Brown, S.C., Jeffs, P.W., Kopple, K.D., Mueller, L.(1990) Biochemistry 29: 7805-7813
- PubMed: 2261437
- DOI: https://doi.org/10.1021/bi00486a005
- Primary Citation of Related Structures:
4TGF - PubMed Abstract:
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by restrained molecular dynamics refinement using NOE distance constraints and some torsion angle constraints derived from J-couplings. Over 80 long-range NOE constraints were found by completely assigning all resolved cross-peaks in the NOESY spectra. Low NOE constraint violations were observed in structures obtained with the following three different refinement procedures: interactive annealing in DSPACE, AMBER 3.0 restrained molecular dynamics, and dynamic simulated annealing in XPLOR. The segment from Phe15 to Asp47 was found to be conformationally well-defined. Back-calculations of NOESY spectra were used to evaluate the quality of the structures. Our calculated structures resemble the ribbon diagram presentations that were recently reported by other groups. Several side-chain conformations appear to be well-defined as does the relative orientation of the C loop to the N-terminal half of the protein.
Organizational Affiliation:
Smith Kline & French Laboratories, King of Prussia, Pennsylvania 19406-0939.
