5T6G: 2.45 A Resolution Structure Of Norovirus 3cl Protease In Complex With The Dipeptidyl Inhibitor 7m (hexagonal Form)

Citation:
Abstract
Human noroviruses are the primary cause of epidemic and sporadic acute gastroenteritis. The worldwide high morbidity and mortality associated with norovirus infections, particularly among the elderly, immunocompromised patients and children, constitute a serious public health concern. There are currently no approved human vaccines or norovirus-specific small-molecule therapeutics or prophylactics. Norovirus 3CL protease has recently emerged as a potential therapeutic target for the development of anti-norovirus agents. We hypothesized that the S4 subsite of the enzyme may provide an effective means of designing potent and cell permeable inhibitors of the enzyme. We report herein the structure-guided exploration and exploitation of the S4 subsite of norovirus 3CL protease in the design and synthesis of effective inhibitors of the protease.
PDB ID: 5T6GDownload
MMDB ID: 145175
PDB Deposition Date: 2016/9/1
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 2.45  Å
Source Organism:
Similar Structures:
Biological Unit for 5T6G: monomeric; determined by author
Molecular Components in 5T6G
Label Count Molecule
Protein (1 molecule)
1
Genome Polyprotein(Gene symbol: ORF1)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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