Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.
- 1 November 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (22) , 8594-8598
- https://doi.org/10.1073/pnas.83.22.8594
Abstract
Epidermal growth factor (EGF) is a small mitogenic protein. Proteins with sequence homology with EGF or with its membrane-bound protein receptor have been proposed to play a role in oncogenesis. This report describes solution NMR data that provide evidence that the solution conformation of murine EGF includes an anti-parallel beta-sheet structure involving residues S2-P4, V19-I23, and S28-N32; a small anti-parallel beta-sheet involving residues Y37-S38 and T44-R45; and a multiple-bend (or short irregular helix) structure for residues C6-C14 that is disulfide bonded to the V19-I23/S28-N32 beta-sheet. Implications of these results for structure and function studies of EGF and for molecular design of EGF and homologous alpha-type transforming growth factors are discussed.This publication has 33 references indexed in Scilit:
- Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2Journal of Molecular Biology, 1986
- Secondary structure of the α-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonanceJournal of Molecular Biology, 1985
- A synthetic fragment of rat transforming growth factor α with receptor binding and antigenic propertiesBiochemical and Biophysical Research Communications, 1985
- Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular proteinJournal of Molecular Biology, 1984
- Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonanceJournal of Molecular Biology, 1984
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Two-dimensional double quantum 1H NMR spectroscopy of proteinsBiochemical and Biophysical Research Communications, 1983
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Autocrine Secretion and Malignant Transformation of CellsNew England Journal of Medicine, 1980