Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch

Mature nonstructural protein-15 (nsp15) from the severe acute respiratory syndrome coronavirus (SARS-CoV) contains a novel uridylate-specific Mn2+-dependent endoribonuclease (NendoU). Structure studies of the full-length form of the obligate hexameric enzyme from two CoVs, SARS-CoV and murine hepati...

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Vydané v:	Journal of virology Ročník 81; číslo 12; s. 6700
Hlavní autori:	Joseph, Jeremiah S, Saikatendu, Kumar Singh, Subramanian, Vanitha, Neuman, Benjamin W, Buchmeier, Michael J, Stevens, Raymond C, Kuhn, Peter
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 01.06.2007
Predmet:	Allosteric Site Animals Binding Sites Catalytic Domain Cloning, Molecular Crystallography, X-Ray Dimerization Electrophoresis, Polyacrylamide Gel Manganese - chemistry Molecular Conformation Mutagenesis Protein Conformation RNA Replicase - chemistry SARS Virus - enzymology Viral Nonstructural Proteins - chemistry Xenopus laevis
ISSN:	0022-538X
On-line prístup:	Zistit podrobnosti o prístupe
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