| FEBS Letters | |
| Solution structure of epiregulin and the effect of its C‐terminal domain for receptor binding affinity | |
| Sato, Katsuharu2  Kawano, Keiichi2  Miura, Kazunori2  Gomi, Tomoharu3  Aizawa, Tomoyasu2  Miyamoto, Kaoru1  Nakamura, Takashi2  Tada, Masahito2  Mizuguchi, Mineyuki2  | |
| [1] Department of Biochemistry, Fukui Medical University, Shimoaizuki, Matsuoka, Fukui 910-1193, Japan;Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan;Scientific Instrument Center, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan | |
| 关键词: Epiregulin; Nuclear magnetic resonance; Epidermal growth factor; Structure; EPR; epiregulin; EGF; epidermal growth factor; BTC; betacellulin; TGF; transforming growth factor; HB-EGF; heparin-binding EGF-like growth factor; HRG; heregulin; HRG-αe; EGF-like domain of HRG-α; BTCe; EGF-like domain of BTC; NMR; nuclear magnetic resonance; Trx; thioredoxin; DQF-COSY; double quantum filtered correlation spectroscopy; TOCSY; total correlation spectroscopy; NOESY; nuclear Overhauser enhancement spectroscopy; NOE; nuclear Overhauser effect; CSI; chemical shift index; SA; simulated annealing; RMSD; root mean square deviation; GBP; growth-blocking peptide; | |
| DOI : 10.1016/S0014-5793(03)01005-6 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020313475ZK.pdf | 397KB |
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