1H, 13C and 15N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2 - Laboratoire d'ingénierie des systèmes macromoléculaires Accéder directement au contenu
Article Dans Une Revue Biomolecular NMR Assignments Année : 2017

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

Résumé

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.
Fichier non déposé

Dates et versions

hal-01791552 , version 1 (17-05-2018)

Identifiants

Citer

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, 2017, 12 (1), pp.23 - 26. ⟨10.1007/s12104-017-9773-4⟩. ⟨hal-01791552⟩
186 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More