Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 70, Issue -, Pages 2401-2412Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1399004714014278
Keywords
-
Funding
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
- Agence Nationale de la Recherche [ANR-08-PCVI-0037-01]
- Association pour la Recherche contre le Cancer (ARC) [A09/4/5005, SFI20121205902]
- Agence Nationale de la Recherche (ANR) [ANR-08-PCVI-0037] Funding Source: Agence Nationale de la Recherche (ANR)
Ask authors/readers for more resources
Protein arginine methyltransferase 7 (PRMT7) is a type III arginine methyltransferase which has been implicated in several biological processes such as transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation and metastasis. PRMT7 is a unique but less characterized member of the family of PRMTs. The crystal structure of full-length PRMT7 from Mus musculus refined at 1.7 angstrom resolution is described. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The high-resolution crystal structure presented here revealed several structural features showing that the second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available