Solution NMR assignment of the ARC4 domain of human tankyrase 2.
ADP-ribosylation
Ankyrin repeats
Signaling
Ubiquitylation
Journal
Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
08
02
2019
accepted:
02
03
2019
pubmed:
9
3
2019
medline:
20
8
2019
entrez:
9
3
2019
Statut:
ppublish
Résumé
Tankyrases are poly(ADP-ribose)polymerases (PARPs) which recognize their substrates via their ankyrin repeat cluster (ARC) domains. The human tankyrases (TNKS/TNKS2) contain five ARCs in their extensive N-terminal region; of these, four bind peptides present within tankyrase interactors and substrates. These short, linear segments, known as tankyrase-binding motifs (TBMs), contain some highly conserved features: an arginine at position 1, which occupies a predominantly acidic binding site, and a glycine at position 6 that is sandwiched between two aromatic side chains on the surface of the ARC domain. Tankyrases are involved in a multitude of biological functions, amongst them Wnt/β-catenin signaling, the maintenance of telomeres, glucose metabolism, spindle formation, the DNA damage response and Hippo signaling. As many of these are relevant to human disease, tankyrase is an important target candidate for drug development. With the emergence of non-catalytic (scaffolding) functions of tankyrase, it seems attractive to interfere with ARC function rather than the enzymatic activity of tankyrase. To study the mechanism of ARC-dependent recruitment of tankyrase binders and enable protein-observed NMR screening methods, we have as the first step obtained a full backbone and partial side chain assignment of TNKS2 ARC4. The assignment highlights some of the unusual structural features of the ARC domain.
Identifiants
pubmed: 30847846
doi: 10.1007/s12104-019-09887-w
pii: 10.1007/s12104-019-09887-w
pmc: PMC6439159
doi:
Substances chimiques
Solutions
0
TNKS2 protein, human
EC 2.4.2.30
Tankyrases
EC 2.4.2.30
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
255-260Subventions
Organisme : Wellcome Trust
ID : WT102360/13/Z
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C47521/A16217
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U117533887
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C309/A11566
Pays : United Kingdom
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