4TGF

SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA

Summary for 4TGF

• Entry DOI: 10.2210/pdb4tgf/pdb
• Descriptor: DES-VAL-1,VAL-2,TRANSFORMING GROWTH FACTOR, ALPHA (1 entity in total)
• Functional Keywords: growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Transforming growth factor alpha: Secreted, extracellular space. Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein: P01135
• Total number of polymer chains: 1
• Total formula weight: 5560.25

Authors

Kline, T.P.,Brown, F.K.,Brown, S.C.,Jeffs, P.W.,Kopple, K.D.,Mueller, L. (deposition date: 1990-06-13, release date: 1991-10-15, Last modification date: 2024-11-20)

Primary citation

Kline, T.P.,Brown, F.K.,Brown, S.C.,Jeffs, P.W.,Kopple, K.D.,Mueller, L.
Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Biochemistry, 29:7805-7813, 1990

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.

PubMed: 2261437
DOI: 10.1021/bi00486a005

Experimental method

SOLUTION NMR