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. 1986 Nov;83(22):8594–8598. doi: 10.1073/pnas.83.22.8594

Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.

G T Montelione, K Wüthrich, E C Nice, A W Burgess, H A Scheraga
PMCID: PMC386977  PMID: 3490668

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.

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Selected References

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