 |
PDBsum entry 4oau
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/RNA
|
PDB id
|
|
|
|
4oau
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase/RNA
|
|
|
Title:
|
|
Complete human rnase l in complex with biological activators.
|
|
Structure:
|
|
2-5a-dependent ribonuclease. Chain: c. Fragment: unp residues 21-719. Synonym: 2-5a-dependent rnase, ribonuclease 4, ribonuclease l, rnase l. Engineered: yes. Mutation: yes. RNA (5'-r(p A Ap A)-2'). Chain: a.
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: rnasel, rns4. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: chemical synthesis
|
|
Resolution:
|
|
|
2.60Å
|
R-factor:
|
0.213
|
R-free:
|
0.251
|
|
|
Authors:
|
|
Y.Han,J.Donovan,S.Rath,G.Whitney,A.Chitrakar,A.Korennykh
|
|
Key ref:
|
|
Y.Han
et al.
(2014).
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response.
Science,
343,
1244-1248.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
06-Jan-14
|
Release date:
|
12-Mar-14
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q05823
(RN5A_HUMAN) -
2-5A-dependent ribonuclease from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
741 a.a.
692 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Science
343:1244-1248
(2014)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response.
|
|
Y.Han,
J.Donovan,
S.Rath,
G.Whitney,
A.Chitrakar,
A.Korennykh.
|
|
|
|
|
| |
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
