4OAU

Complete human RNase L in complex with biological activators.

Summary for 4OAU

• Entry DOI: 10.2210/pdb4oau/pdb
• Related: 4OAV
• Descriptor: 2-5A-dependent ribonuclease, RNA (5'-R(P*A*AP*A)-2'), ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: rnase l, rnasel, 2-5a, 2', 5'-oligoadenylate, interferon, ken, pseudokinase, kinase, inflammation, ire1, ridd, regulated rna decay, splicing cleavage, hpc1, hereditary prostate cancer 1, rnase l kinase-homology and ken domain-containing, innate immunity, interferon response, antiviral response, 2-5a (2', 5'-linked oligoadenylate)and rna, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q05823
• Total number of polymer chains: 2
• Total formula weight: 80834.82

Authors

Han, Y.,Donovan, J.,Rath, S.,Whitney, G.,Chitrakar, A.,Korennykh, A. (deposition date: 2014-01-06, release date: 2014-03-12, Last modification date: 2024-02-28)

Primary citation

Han, Y.,Donovan, J.,Rath, S.,Whitney, G.,Chitrakar, A.,Korennykh, A.
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response.
Science, 343:1244-1248, 2014

PubMed Abstract: One of the hallmark mechanisms activated by type I interferons (IFNs) in human tissues involves cleavage of intracellular RNA by the kinase homology endoribonuclease RNase L. We report 2.8 and 2.1 angstrom crystal structures of human RNase L in complexes with synthetic and natural ligands and a fragment of an RNA substrate. RNase L forms a crossed homodimer stabilized by ankyrin (ANK) and kinase homology (KH) domains, which positions two kinase extension nuclease (KEN) domains for asymmetric RNA recognition. One KEN protomer recognizes an identity nucleotide (U), whereas the other protomer cleaves RNA between nucleotides +1 and +2. The coordinated action of the ANK, KH, and KEN domains thereby provides regulated, sequence-specific cleavage of viral and host RNA targets by RNase L.

PubMed: 24578532
DOI: 10.1126/science.1249845

Experimental method

X-RAY DIFFRACTION (2.6 Å)