Conformational flexibility of GRASPs and their constituent PDZ subdomains reveals structural basis of their promiscuous interactome.
ABF simulation
GRASP
NMR
PDZ asymmetry
molten globule
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
29
06
2019
revised:
19
11
2019
accepted:
08
01
2020
pubmed:
11
1
2020
medline:
14
5
2021
entrez:
11
1
2020
Statut:
ppublish
Résumé
The Golgi complex is a central component of the secretory pathway, responsible for several critical cellular functions in eukaryotes. The complex is organized by the Golgi matrix that includes the Golgi reassembly and stacking protein (GRASP), which was shown to be involved in cisternae stacking and lateral linkage in metazoan. GRASPs also have critical roles in other processes, with an unusual ability to interact with several different binding partners. The conserved N terminus of the GRASP family includes two PSD-95, DLG, and ZO-1 (PDZ) domains. Previous crystallographic studies of orthologues suggest that PDZ1 and PDZ2 have similar conformations and secondary structure content. However, PDZ1 alone mediates nearly all interactions between GRASPs and their partners. In this work, NMR, synchrotron radiation CD, and molecular dynamics (MD) were used to examine the structure, flexibility, and stability of the two constituent PDZ domains. GRASP PDZs are structured in an unusual β
Substances chimiques
Golgi Matrix Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3255-3272Subventions
Organisme : BBSRC
ID : BB/N006011/1
Organisme : Wellcome Trust
ID : 20289/Z16/Z
Pays : United Kingdom
Informations de copyright
© 2020 Federation of European Biochemical Societies.
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