6B6I
2.4A resolution structure of human Norovirus GII.4 protease
Summary for 6B6I
| Entry DOI | 10.2210/pdb6b6i/pdb |
| Descriptor | 3C-like protease (2 entities in total) |
| Functional Keywords | 3c-like protease, viral protease, gii.4, minerva, viral protein, protease |
| Biological source | Norovirus GII.4 |
| Total number of polymer chains | 8 |
| Total formula weight | 153937.38 |
| Authors | Muzzarelli, K.M.,Kuiper, B.D.,Spellmon, N.S.,Hackett, J.,Brunzelle, J.S.,Kovari, I.A.,Amblard, F.,Yang, Z.,Schinazi, R.F.,Kovari, L.C. (deposition date: 2017-10-02, release date: 2018-10-03, Last modification date: 2023-10-04) |
| Primary citation | Muzzarelli, K.M.,Kuiper, B.,Spellmon, N.,Brunzelle, J.,Hackett, J.,Amblard, F.,Zhou, S.,Liu, P.,Kovari, I.A.,Yang, Z.,Schinazi, R.F.,Kovari, L.C. Structural and Antiviral Studies of the Human Norovirus GII.4 Protease. Biochemistry, 58:900-907, 2019 Cited by PubMed Abstract: Norovirus is the leading cause of acute gastroenteritis worldwide with a yearly reported 700 million cases driving a $60 billion global socioeconomic burden. With no United States Food and Drug Administration approved therapeutics and the chance for severe chronic infection and life-threatening complications, researchers have identified the protease as a potential target. However, drug development has focused on the norovirus GI.1 strain despite its accounting for less than 5% of all outbreaks. Our lab aims to change focus for norovirus drug design from GI.1 to the highly infective GII.4, responsible for more than 50% of all outbreaks worldwide. With the first published crystal structure of the norovirus GII.4 protease, we have identified several significant differences in the structure and active site that have hindered development of a potent inhibitor targeting the norovirus GII.4 protease. With these new insights, we have begun designing compounds that demonstrate increased inhibition of the clinically most relevant norovirus GII.4 strain. PubMed: 30605321DOI: 10.1021/acs.biochem.8b01063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.44 Å) |
Structure validation
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