PMID- 16855311
OWN - NLM
STAT- MEDLINE
DCOM- 20060915
LR  - 20150813
IS  - 0907-4449 (Print)
IS  - 0907-4449 (Linking)
VI  - 62
IP  - Pt 8
DP  - 2006 Aug
TI  - Structural basis for non-catalytic and catalytic activities of ribonuclease III.
PG  - 933-40
AB  - Ribonuclease III (RNase III) represents a highly conserved family of 
      double-stranded (ds) RNA-specific endoribonucleases, exemplified by bacterial 
      RNase III and eukaryotic Rnt1p, Drosha and Dicer. Bacterial RNase III, containing 
      an endonuclease domain followed by a dsRNA-binding domain, is the most 
      extensively studied member of the family. It can affect RNA structure and gene 
      expression in either of two ways: as a processing enzyme that cleaves dsRNA or as 
      a binding protein that binds but does not cleave dsRNA. The available biochemical 
      and structural data support the existence of two distinct forms of the RNase 
      III-dsRNA complex which reflect the dual activities of the protein. The 
      information revealed by the structures of bacterial RNase III provides insight 
      into the mechanism of dsRNA processing by all members of the family.
FAU - Ji, Xinhua
AU  - Ji X
AD  - Macromolecular Crystallography Laboratory, National Cancer Institute, National 
      Institutes of Health, Frederick, MD 21702, USA. jix@ncifcrf.gov
LA  - eng
GR  - Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
PT  - Review
DEP - 20060718
PL  - United States
TA  - Acta Crystallogr D Biol Crystallogr
JT  - Acta crystallographica. Section D, Biological crystallography
JID - 9305878
RN  - 0 (RNA, Double-Stranded)
RN  - EC 3.1.26.3 (Ribonuclease III)
SB  - IM
MH  - Animals
MH  - Gene Expression
MH  - Humans
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - RNA Processing, Post-Transcriptional/*physiology
MH  - RNA, Double-Stranded/chemistry/*metabolism
MH  - Ribonuclease III/chemistry/*metabolism
MH  - Structure-Activity Relationship
RF  - 43
EDAT- 2006/07/21 09:00
MHDA- 2006/09/16 09:00
CRDT- 2006/07/21 09:00
PHST- 2006/01/31 00:00 [received]
PHST- 2006/03/29 00:00 [accepted]
PHST- 2006/07/21 09:00 [pubmed]
PHST- 2006/09/16 09:00 [medline]
PHST- 2006/07/21 09:00 [entrez]
AID - S090744490601153X [pii]
AID - 10.1107/S090744490601153X [doi]
PST - ppublish
SO  - Acta Crystallogr D Biol Crystallogr. 2006 Aug;62(Pt 8):933-40. doi: 
      10.1107/S090744490601153X. Epub 2006 Jul 18.