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

doi:10.1073/pnas.83.22.8594

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

Research output: Contribution to journal › Article › Research › peer-review

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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 language	English
Pages (from-to)	8594-8598
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	83
Issue number	22
DOIs	https://doi.org/10.1073/pnas.83.22.8594
Publication status	Published - 1 Dec 1986
Externally published	Yes

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Montelione, G. T., Wuthrich, K., Nice, E. C., Burgess, A. W., & Scheraga, H. A. (1986). Identification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance. Proceedings of the National Academy of Sciences of the United States of America, 83(22), 8594-8598. https://doi.org/10.1073/pnas.83.22.8594

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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.",

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Montelione, GT, Wuthrich, K, Nice, EC, Burgess, AW & Scheraga, HA 1986, 'Identification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance', Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 22, pp. 8594-8598. https://doi.org/10.1073/pnas.83.22.8594

Identification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance. / Montelione, G. T.; Wuthrich, K.; Nice, E. C. et al.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 22, 01.12.1986, p. 8594-8598.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Identification of two anti-parallel β-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance

AU - Montelione, G. T.

AU - Wuthrich, K.

AU - Nice, E. C.

AU - Burgess, A. W.

AU - Scheraga, H. A.

PY - 1986/12/1

Y1 - 1986/12/1

N2 - 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.

AB - 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.

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

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