Skip to Main content Skip to Navigation
Journal articles

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

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.
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-01791552
Contributor : Louciné Mitoyan Connect in order to contact the contributor
Submitted on : Thursday, May 17, 2018 - 3:26:20 PM
Last modification on : Tuesday, October 19, 2021 - 10:59:15 PM

Identifiers

Citation

Yinghui Wang, Louise Pinet, Nadine Assrir, Latifa Elantak, Francoise Guerlesquin, et al.. 1H, 13C and 15N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2. Biomolecular NMR Assignments, Springer, 2017, 12 (1), pp.23 - 26. ⟨10.1007/s12104-017-9773-4⟩. ⟨hal-01791552⟩

Share

Metrics

Record views

187