Peptidase S1, PA clan, chymotrypsin-like fold
Short name | Peptidase_S1_PA_chymotrypsin |
Overlapping entries |
Description
References
1.Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic. Lubin JH, Zardecki C, Dolan EM, Lu C, Shen Z, Dutta S, Westbrook JD, Hudson BP, Goodsell DS, Williams JK, Voigt M, Sarma V, Xie L, Venkatachalam T, Arnold S, Alfaro Alvarado LH, Catalfano K, Khan A, McCarthy E, Staggers S, Tinsley B, Trudeau A, Singh J, Whitmore L, Zheng H, Benedek M, Currier J, Dresel M, Duvvuru A, Dyszel B, Fingar E, Hennen EM, Kirsch M, Khan AA, Labrie-Cleary C, Laporte S, Lenkeit E, Martin K, Orellana M, Ortiz-Alvarez de la Campa M, Paredes I, Wheeler B, Rupert A, Sam A, See K, Soto Zapata S, Craig PA, Hall BL, Jiang J, Koeppe JR, Mills SA, Pikaart MJ, Roberts R, Bromberg Y, Hoyer JS, Duffy S, Tischfield J, Ruiz FX, Arnold E, Baum J, Sandberg J, Brannigan G, Khare SD, Burley SK. Proteins (2021). PMID: 34580920
2.X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease. Science 372, 642-646, (2021). PMID: 33811162
3.Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Bazan JF, Fletterick RJ. Proc. Natl. Acad. Sci. U.S.A. 85, 7872-6, (1988). View articlePMID: 3186696
4.Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors. Shi J, Wei Z, Song J. J. Biol. Chem. 279, 24765-73, (2004). PMID: 15037623
5.Structures of two coronavirus main proteases: implications for substrate binding and antiviral drug design. Xue X, Yu H, Yang H, Xue F, Wu Z, Shen W, Li J, Zhou Z, Ding Y, Zhao Q, Zhang XC, Liao M, Bartlam M, Rao Z. J. Virol. 82, 2515-27, (2008). View articlePMID: 18094151
6.Picornaviral 3C protease inhibitors and the dual 3C protease/coronaviral 3C-like protease inhibitors. Wang HM, Liang PH. Expert Opin Ther Pat 20, 59-71, (2010). PMID: 20021285
7.Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Anand K, Ziebuhr J, Wadhwani P, Mesters JR, Hilgenfeld R. Science 300, 1763-7, (2003). View articlePMID: 12746549
8.Structure of the main protease from a global infectious human coronavirus, HCoV-HKU1. Zhao Q, Li S, Xue F, Zou Y, Chen C, Bartlam M, Rao Z. J. Virol. 82, 8647-55, (2008). View articlePMID: 18562531
9.Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. Anand K, Palm GJ, Mesters JR, Siddell SG, Ziebuhr J, Hilgenfeld R. EMBO J. 21, 3213-24, (2002). View articlePMID: 12093723
Cross References
ENZYME
- 2.1.1.-
- 2.1.1.56
- 2.1.1.57
- 2.7.7.48
- 2.7.7.50
- 3.1.13.-
- 3.4.14.-
- 3.4.19.12
- 3.4.21.-
- 3.4.21.1
- 3.4.21.10
- 3.4.21.104
- 3.4.21.106
- 3.4.21.107
- 3.4.21.109
- 3.4.21.117
- 3.4.21.118
- 3.4.21.119
- 3.4.21.12
- 3.4.21.120
- 3.4.21.122
- 3.4.21.19
- 3.4.21.2
- 3.4.21.20
- 3.4.21.21
- 3.4.21.22
- 3.4.21.27
- 3.4.21.32
- 3.4.21.34
- 3.4.21.35
- 3.4.21.36
- 3.4.21.37
- 3.4.21.38
- 3.4.21.39
- 3.4.21.4
- 3.4.21.41
- 3.4.21.42
- 3.4.21.43
- 3.4.21.45
- 3.4.21.46
- 3.4.21.49
- 3.4.21.5
- 3.4.21.50
- 3.4.21.54
- 3.4.21.59
- 3.4.21.6
- 3.4.21.68
- 3.4.21.69
- 3.4.21.7
- 3.4.21.70
- 3.4.21.71
- 3.4.21.73
- 3.4.21.74
- 3.4.21.76
- 3.4.21.77
- 3.4.21.78
- 3.4.21.79
- 3.4.21.80
- 3.4.21.81
- 3.4.21.82
- 3.4.21.84
- 3.4.21.85
- 3.4.21.86
- 3.4.21.9
- 3.4.21.90
- 3.4.21.91
- 3.4.21.95
- 3.4.21.98
- 3.4.21.99
- 3.4.22.-
- 3.4.22.28
- 3.4.22.29
- 3.4.22.44
- 3.4.22.45
- 3.4.22.46
- 3.4.22.66
- 3.4.22.69
- 3.4.25.-
- 3.6.1.15
- 3.6.4.-
- 3.6.4.12
- 3.6.4.13
- 4.6.1.-
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:2.40.10.10