Publication Date:
2006-06-17
Description:
Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albertini, Aurelie A V -- Wernimont, Amy K -- Muziol, Tadeusz -- Ravelli, Raimond B G -- Clapier, Cedric R -- Schoehn, Guy -- Weissenhorn, Winfried -- Ruigrok, Rob W H -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):360-3. Epub 2006 Jun 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Virologie Moleculaire et Structurale, FRE 2854 Universite Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778023" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Crystallography, X-Ray
;
DNA-Directed RNA Polymerases/metabolism
;
Genome, Viral
;
Models, Molecular
;
Molecular Sequence Data
;
Nucleic Acid Conformation
;
Nucleocapsid Proteins/*chemistry/metabolism
;
Phosphoproteins/metabolism
;
Phosphorylation
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Quaternary
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Subunits/chemistry
;
RNA, Viral/*chemistry/genetics/metabolism
;
Rabies virus/*chemistry/genetics
;
Recombinant Proteins/chemistry
;
Ribonucleoproteins/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
