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2N5K

Regnase-1 Zinc finger domain

Summary for 2N5K
Entry DOI10.2210/pdb2n5k/pdb
Related2N5J 2N5L
NMR InformationBMRB: 25719
DescriptorRibonuclease ZC3H12A, ZINC ION (2 entities in total)
Functional Keywordsregnase, regnase-1, zc3h12a, zinc finger, hydrolase
Biological sourceMus musculus (mouse)
Cellular locationCytoplasm : Q5D1E7
Total number of polymer chains1
Total formula weight3555.48
Authors
Yokogawa, M.,Tsushima, T.,Noda, N.N.,Kumeta, H.,Adachi, W.,Enokizono, Y.,Yamashita, K.,Standley, D.M.,Takeuchi, O.,Akira, S.,Inagaki, F. (deposition date: 2015-07-18, release date: 2016-03-16, Last modification date: 2024-10-30)
Primary citationYokogawa, M.,Tsushima, T.,Noda, N.N.,Kumeta, H.,Enokizono, Y.,Yamashita, K.,Standley, D.M.,Takeuchi, O.,Akira, S.,Inagaki, F.
Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions
Sci Rep, 6:22324-22324, 2016
Cited by
PubMed Abstract: Regnase-1 is an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. Here, we report the structures of four domains of Regnase-1 from Mus musculus-the N-terminal domain (NTD), PilT N-terminus like (PIN) domain, zinc finger (ZF) domain and C-terminal domain (CTD). The PIN domain harbors the RNase catalytic center; however, it is insufficient for enzymatic activity. We found that the NTD associates with the PIN domain and significantly enhances its RNase activity. The PIN domain forms a head-to-tail oligomer and the dimer interface overlaps with the NTD binding site. Interestingly, mutations blocking PIN oligomerization had no RNase activity, indicating that both oligomerization and NTD binding are crucial for RNase activity in vitro. These results suggest that Regnase-1 RNase activity is tightly controlled by both intramolecular (NTD-PIN) and intermolecular (PIN-PIN) interactions.
PubMed: 26927947
DOI: 10.1038/srep22324
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Experimental method
SOLUTION NMR
Structure validation

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