Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell growth, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), which is a competitor for EGF receptor sites. EGF is a small 53 amino acid residue long protein that contains three disulfide briges.
EGF is colored by secondary structure.

The three disulfide bridges are colored yellow and are as folows: Cys6-Cys20, Cys14-Cys31, and Cys33-Cys42. The protein itself is colored by chain. The side chains of residues 13 (Tyr),41 (Arg), and 47 (Leu) are all thought to play an important role in EGF's functionality.

Another conformer of EGF

• Keywords: EGF-like Domain, Repeat, Growth Factor, Transmembrane, Glycoprotein, Signal
• View this protein's PDB entry as 3EGF
• View this protein's entry in the SwissProt database as EGF_MOUSE
• References
  • G.T. Montelione, K. Wuthrich, A.W. Burgess, E.C.Nice, G. Wagner, K.D. Gibson, H.A. Scheraga
    Solution Structure of Murine Epidermal Growth Factor Determined by NMR Spectroscopy and Refined by Energy Minimization with Restraints.
    Biochemistry 31:236 (1992)
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  • G.T. Montelione, K. Wuthrich, H.A. Scheraga
    Sequence-Specific 1H NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor.
    Biochemistry 27:2235 (1988)
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  • G.T. Montelione, K. Wuthrich, E.C. Nice, A.W. Burgess, H.A. Scheraga
    Solution Structure of Murine Epidermal Growth Factor: Determination of the Polypeptide Backbone Chain-Fold by Nuclear Magnetic Resonance and Distance Geometry.
    Proc.Nat.Acad.Sci.USA 84:5226 (1987)
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  • G.T. Montelione, K. Wuthrich, E.C. Nice, A.W. Burgess, H.A. Scheraga
    Identification of Two Anti-Parallel Beta-Sheet Conformations in the Solution Structure of Murine Epidermal Growth Factor by Proton Magnetic Resonance.
    Proc.Nat.Acad.Sci.USA 83:8594 (1986)
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