Microscale thermophoresis analysis of the molecular interaction between small nuclear ribonucleoprotein polypeptide G and the RING finger domain of RBBP6 towards anti-cancer drug discovery.
Anti-cancer drug discovery
RBBP6
RING finger
SNPRG
cancer
microscale thermophoresis
Journal
American journal of translational research
ISSN: 1943-8141
Titre abrégé: Am J Transl Res
Pays: United States
ID NLM: 101493030
Informations de publication
Date de publication:
2021
2021
Historique:
received:
16
05
2021
accepted:
16
08
2021
entrez:
27
12
2021
pubmed:
28
12
2021
medline:
28
12
2021
Statut:
epublish
Résumé
Regulatory core-splicing proteins are now becoming highly promising therapeutic targets for the development of anti-cancer drugs. SNRPG and RBBP6 are two good examples of regulatory core-splicing proteins involved in tumorigenesis and tumor development whose multi-functional role is primarily mediated by protein-protein interactions. Over the years, skepticism abutting from the two onco-proteins has been mounting. Suggestive evidence using yeast 2-hybrid technique observed possible involvement between SNRPG and the RING finger domain of RBBP6. However, the putative interaction remains elusive and yet to be characterized. In this study, we developed the first MST-based assay to confirm the interaction between SNRPG and the RING finger domain of RBBP6. The results demonstrated a strong binding affinity between SNRPG and the RING finger domain of RBBP6 with a K
Types de publication
Journal Article
Langues
eng
Pagination
12775-12785Informations de copyright
AJTR Copyright © 2021.
Déclaration de conflit d'intérêts
None.
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