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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
09:16

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

The solution structure of human epidermal growth factor.

R M Cooke, A J Wilkinson, M Baron

    Nature
    |May 3, 1987
    PubMed
    Summary

    Researchers determined the 3D structure of a human epidermal growth factor (hEGF) derivative using NMR. This structure helps understand EGF properties and predict related protein structures.

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    Validated Immunochemical Assay for Comprehensive Determination of the Human Epidermal Growth Factor Receptor 2 Released from and Bound to Cells

    Published on: May 9, 2025

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Molecular Biology

    Background:

    • Epidermal Growth Factors (EGFs) are potent mitogens with roles in cell growth.
    • Human EGF (hEGF), also known as urogastrone, inhibits gastric acid secretion.
    • EGF-like sequences appear in diverse proteins, but EGF structure determination is challenging due to crystallization difficulties.

    Purpose of the Study:

    • To determine the three-dimensional structure of a biologically active fragment of human EGF.
    • To provide a structural basis for understanding EGF family properties.
    • To aid in predicting the structures of homologous sequences in other proteins.

    Main Methods:

    • High-resolution 1H nuclear magnetic resonance (NMR) spectroscopy was employed.
    • Distance geometry calculations were utilized.
    • Restrained energy minimization and restrained molecular dynamics methods were applied.

    Main Results:

    • A three-dimensional structure for residues 1-48 of human EGF was successfully determined.
    • The determined structure represents a biologically active derivative of hEGF.
    • The structural data offers insights into the molecular conformation of EGF.

    Conclusions:

    • The determined 3D structure of hEGF provides a foundation for understanding EGF family functions.
    • This structural information can guide the prediction of structures for proteins with EGF-like domains.
    • The study overcomes previous limitations in determining EGF structure by diffraction methods.