Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP.
BCH domain
GTPase-activating protein
Rho
Scaffold
Structure
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
13 May 2024
13 May 2024
Historique:
received:
25
10
2023
accepted:
11
04
2024
revised:
08
04
2024
medline:
14
5
2024
pubmed:
14
5
2024
entrez:
13
5
2024
Statut:
epublish
Résumé
p50RhoGAP is a key protein that interacts with and downregulates the small GTPase RhoA. p50RhoGAP is a multifunctional protein containing the BNIP-2 and Cdc42GAP Homology (BCH) domain that facilitates protein-protein interactions and lipid binding and the GAP domain that regulates active RhoA population. We recently solved the structure of the BCH domain from yeast p50RhoGAP (
Identifiants
pubmed: 38740643
doi: 10.1007/s00018-024-05238-8
pii: 10.1007/s00018-024-05238-8
doi:
Substances chimiques
Proline
9DLQ4CIU6V
Tyrosine
42HK56048U
Saccharomyces cerevisiae Proteins
0
rhoA GTP-Binding Protein
EC 3.6.5.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
216Subventions
Organisme : Ministry of Education - Singapore
ID : R154-000-C07-114
Organisme : Ministry of Education - Singapore
ID : A-8000477-00-00
Organisme : Ministry of Education - Singapore
ID : AcRF Tier 3 Grant MOE 2016-T3-1-002
Informations de copyright
© 2024. The Author(s).
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