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

G. T. Montelione, K. Wuthrich, E. C. Nice, A. W. Burgess, H. A. Scheraga

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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 β-sheet structure involving residues S2-P4, V19-I23, and S28-N32; a small anti-parallel β-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 β-sheet. Implications of these results for structure and function studies of EGF and for molecular design of EGF and homologous α-type transforming growth factors are discussed.

Original languageEnglish
Pages (from-to)8594-8598
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number22
DOIs
Publication statusPublished - 1 Dec 1986
Externally publishedYes

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