Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch. [electronic resource]
Producer: 20070711Description: 6700-8 p. digitalISSN:- 0022-538X
- Allosteric Site
- Animals
- Binding Sites
- Catalytic Domain
- Cloning, Molecular
- Crystallography, X-Ray
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Endoribonucleases
- Manganese -- chemistry
- Molecular Conformation
- Mutagenesis
- Protein Conformation
- RNA-Dependent RNA Polymerase -- chemistry
- Severe acute respiratory syndrome-related coronavirus -- enzymology
- Viral Nonstructural Proteins -- chemistry
- Xenopus laevis
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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