Crystal Structure of Human Epidermal Growth Factor and Its Dimerization
| Autor: | Ji-Jie Chai, Ru-Chang Bi, He-Shu Lu, Bingren Huang, Cun-Heng He, Ming Li |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy Epidermal Growth Factor Human epidermal growth factor Dimer Peptide Cell Biology Nuclear magnetic resonance spectroscopy Crystal structure Hydrogen-Ion Concentration Biology Biochemistry chemistry.chemical_compound chemistry Epidermal growth factor Biophysics Humans Molecule Crystallization Receptor Dimerization Molecular Biology hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of Biological Chemistry. 276:34913-34917 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m102874200 |
| Popis: | Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure. |
| Databáze: | OpenAIRE |
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