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Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4.

Nagata K, Kohda D, Hatanaka H, Ichikawa S, Matsuda S, Yamamoto T, Suzuki A, Inagaki F
EMBO J 13 3517-23 (1994)
Cited: 28 times
EuropePMC logo PMID: 8062828

Abstract

p185erbB-2 and p180erbB-4 are epidermal growth factor (EGF) receptor-like tyrosine kinases, whose co-expression is observed in many breast carcinomas. Heregulins (HRGs), which contain an immunoglobulin unit and an EGF-like domain, bind to p180erbB-4 and activate p180erbB-4 and p185erbB-2 through transphosphorylation or receptor heterodimerization. The EGF-like domain is sufficient for the activation. Despite the sequence similarity, no cross activity is seen between the p180erbB-4 ligands (HRGs) and the p170erbB-1 ligands [EGF and transforming growth factor (TGF)-alpha]. To investigate the structural basis of receptor specificity, we have determined the solution structure of the EGF-like domain of HRG-alpha by two-dimensional 1H nuclear magnetic resonance spectroscopy and simulated annealing calculations. Though its main-chain fold is similar to those of EGF and TGF-alpha, distinctive structural features are observed on the molecular surface including an ionic cluster and hydrophobic patches, which afford HRG-alpha the specific affinity for p180erbB-4. The structure should provide a basis for the structure-activity relationship of HRGs and for the design of drugs which prevent progression of breast cancer.

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Reviews citing this publication (6)

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Articles citing this publication (21)

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  18. Exploring the Binding Mechanism of NRG1-ERBB3 Complex and Discovery of Potent Natural Products to Reduce Diabetes-Assisted Breast Cancer Progression. Marafie SK, Alshawaf E, Abu-Farha M, Thanaraj TA, Wei DQ, Al-Mulla F, Khan A, Abubaker J, Mohammad A. Interdiscip Sci 15 452-464 (2023)
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  20. Fmoc-based solid phase chemical synthesis of 71-meric neuregulin 1-beta1, an epidermal growth factor-like domain. Kakizawa T, Koide-Yoshida S, Kimura T, Uchimura H, Hayashi Y, Saito K, Kiso Y. J Pept Sci 14 261-266 (2008)
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