Virus protease

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<StructureSection load='' size='350' side='right' caption='HIV-1 protease dimer complex with tert-butylcarbonate (PDB entry [[1odw]])' scene='44/443708/Cv/2'>
 
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'''Virus proteases''' include HIV protease, XMRV protease, retropepsin.
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<StructureSection load='' size='350' side='right' caption='Structure of human rhinovirus 3C protease complex with inhibitor (PDB entry [[1cqq]])' scene='55/554890/Cv/1'>
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HIV Protease (HIV-PR) and xenotropic murine leukemia virus protease (XMRV-PR) cleave polyproteins to produce the mature proteins of the virus<ref>PMID:12475203</ref>. Both are aspartyl proteases. The inhibition of HIV-PR results in an uninfectious HIV virion. HIV-1 is found globally while HIV-2, which has lower virulence, is found in West Africa.
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__TOC__
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*<scene name='44/443708/Cv/3'>HIV-1 protease dimer complex with inhibitor tert-butylcarbonate </scene>.
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== Function ==
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*<scene name='44/443708/Cv/5'>Inhibitor BMS-182193 binding site</scene>.
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'''3C protease''' (3CP) is a virus cysteine protease which has essential role in viral replication. 3CP cleaves the precursor viral polyprotein to produce functional proteins and enzymes.<ref>PMID:17305557</ref> For more details on Foot and Mouth Disease virus 3C protease see [[FMDV 3C]].
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== Disease ==
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3CP is an attractive target for therapeutic agents for treatment of diseases caused by the common cold virus. Coxsakievirus causes the human diseases myocarditis and pericarditis.
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== Structural highlights ==
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3CP - a Cys protease fold is similar to that of trypsin-like serine proteases. The <scene name='55/554890/Cv/6'>active site triad contains Cys147, His40 and Glu71</scene> (PDB entry [[1cqq]]).<ref>PMID:10500114</ref> <scene name='55/554890/Cv/5'>Whole binding site</scene>.
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See also<br />
See also<br />
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*'''Foot-and-Mouth Disease virus protease'''
*'''Foot-and-Mouth Disease virus protease'''
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**[[2bhg]] – FMDV – Foot-and-mouth disease virus
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**[[2bhg]] – FMDV residues 1650-1857 (mutant) – Foot-and-mouth disease virus
*'''Infectious Bronchitis virus protease'''
*'''Infectious Bronchitis virus protease'''

Revision as of 16:29, 8 October 2018

Structure of human rhinovirus 3C protease complex with inhibitor (PDB entry 1cqq)

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3D Structures of Virus proteases

Updated on 08-October-2018

References

  1. ↑ Wanga QM, Chen SH. Human rhinovirus 3C protease as a potential target for the development of antiviral agents. Curr Protein Pept Sci. 2007 Feb;8(1):19-27. PMID:17305557
  2. ↑ Matthews DA, Dragovich PS, Webber SE, Fuhrman SA, Patick AK, Zalman LS, Hendrickson TF, Love RA, Prins TJ, Marakovits JT, Zhou R, Tikhe J, Ford CE, Meador JW, Ferre RA, Brown EL, Binford SL, Brothers MA, DeLisle DM, Worland ST. Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11000-7. PMID:10500114

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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