Insight into the C-terminal SH3 domain mediated binding of Drosophila Drk to Sos and Dos.
Daughter of sevenless
Drk
Drosophila
NMR
SH3 domain
Son of sevenless
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
15 10 2022
15 10 2022
Historique:
received:
22
07
2022
accepted:
03
08
2022
pubmed:
12
8
2022
medline:
3
9
2022
entrez:
11
8
2022
Statut:
ppublish
Résumé
Drk, a Drosophila homologue of human GRB2, interacts with Sevenless (Sev) receptor via its SH2 domain, while the N- and C-terminal SH3 domains (Drk-NSH3 and Drk-CSH3, respectively) are responsible for the interaction with proline-rich motifs (PRMs) of Son of sevenless (Sos) or Daughter of Sevenless (Dos). Drk-NSH3 on its own has a conformational equilibrium between folded and unfolded states, and the folded state is stabilised by the association with a Sos-derived proline-rich peptide with PxxPxR motif. In contrast, Drk-CSH3 is supposed to bind PxxxRxxKP motifs in Dos. Aiming at clarifying the structural and functional differences between the two SH3 domains, we performed NMR studies of Drk-CSH3. The resulting solution structure and the
Identifiants
pubmed: 35952612
pii: S0006-291X(22)01112-3
doi: 10.1016/j.bbrc.2022.08.007
pii:
doi:
Substances chimiques
GRB2 Adaptor Protein
0
Peptides
0
Son of Sevenless Proteins
0
Proline
9DLQ4CIU6V
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
87-93Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.