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| {{STRUCTURE_2gth| PDB=2gth | SCENE= }} | | {{STRUCTURE_2gth| PDB=2gth | SCENE= }} |
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| '''crystal structure of the wildtype MHV coronavirus non-structural protein nsp15'''
| | ===crystal structure of the wildtype MHV coronavirus non-structural protein nsp15=== |
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| ==Overview==
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| The unique coronavirus transcription/replication machinery comprised of multiple virus-encoded nonstructural proteins (nsp) plays a vital role during initial and intermediate phases of the viral life cycle. The crystal structure of mouse hepatitis virus strain A59 (MHV-A59) nsp15 is reported at 2.15-A resolution. nsp15 is an XendoU endoribonuclease and is the first one from this family to have its structure unveiled. The MHV-A59 nsp15 monomer structure has a novel protein fold. Two nsp15 trimers form a back-to-back hexamer that is believed to be the functional unit. The structure reveals the catalytic site including the highly conserved residues His262, His277, and Lys317, which is supported by mutagenesis analysis. Gel filtration and enzyme activity assays confirmed that the hexamer is the active form for nsp15 and demonstrate the specificity of nsp15 for uridylate. The high sequence conservation of nsp15 in coronaviruses, including that of severe acute respiratory syndrome, suggests that this protein may provide a new target for the design of antiviral therapeutics. | | The line below this paragraph, {{ABSTRACT_PUBMED_16873248}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16873248 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16873248}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mhv]] | | [[Category: Mhv]] |
| [[Category: Nsp15]] | | [[Category: Nsp15]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:30:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:23:14 2008'' |
