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. 2018 Apr;12(1):23-26.
doi: 10.1007/s12104-017-9773-4. Epub 2017 Sep 13.

1H, 13C and 15N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2

YingHui Wang  1 , Louise Pinet  1 , Nadine Assrir  1 , Latifa Elantak  2 , Françoise Guerlesquin  2 , Ali Badache  3 , Ewen Lescop  1 , Carine van Heijenoort  4
Affiliations
Free article

1H, 13C and 15N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2

YingHui Wang et al. Biomol NMR Assign. 2018 Apr.
Free article

Abstract

ErbB2 (or HER2) is a receptor tyrosine kinase that is involved in signaling pathways controlling cell division, motility and apoptosis. Though important in development and cell growth homeostasis, this protein, when overexpressed, participates in triggering aggressive HER2+ breast cancers. It is composed of an extracellular part and a transmembrane domain, both important for activation by dimerization, and a cytosolic tyrosine kinase, which activates its intrinsically disordered C-terminal end (CtErbB2). Little is known about this C-terminal part of 268 residues, despite its crucial role in interacting with adaptor proteins involved in signaling. Understanding its structural and dynamic characteristics could eventually lead to the design of new interaction inhibitors, and treatments complementary to those already targeting other parts of ErbB2. Here we report backbone and side-chain assignment of CtErbB2, which, together with structural predictions, confirms its intrinsically disordered nature.

Keywords: Breast cancer; ErbB2; Intrinsically disordered protein; Receptor tyrosine kinase.

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References

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