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Virus protease

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[[Image:1odw.png|left|200px|thumb|Crystal Structure of HIV-1 protease [[1odw]]]]
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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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{{STRUCTURE_1odw| PDB=1odw | SIZE=300| S |right|CAPTION=HIV-1 protease [[1odw]] }}
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__TOC__
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== Function ==
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'''Virus protease''' or '''3C protease''' or '''virus proteinase''' are virus cysteine proteases which have essential role in viral replication. The protease cleaves the precursor viral polyprotein to produce functional proteins and enzymes.<ref>PMID:17305557</ref> F
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'''Virus proteases''' include HIV protease, XMRV protease, retropepsin.
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== Disease ==
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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. 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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Virus proteases are 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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{{TOC limit|limit=2}}
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== Structural highlights ==
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Viral protease - 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 />
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*[[Immunodeficiency virus protease]]<br />
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*[[Human Immunodeficiency Virus]]<br />
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*[[HIV-1 protease]]<br />
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*[[HIV Protease Inhibitor Pharmacokinetics]]<br />
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*[[HIV Protease Inhibitor Resistance Profile]]<br />
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*[[HIV Protease Resistance]] <br />
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*[[Molecular Playground/Dengue Virus Protease]]<br />
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*[[Viability of a drug-resistant HIV-1 protease mutant]]<br />
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*[[FMDV 3C]] for Foot-and-Mouth virus protease<br />
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*[[SARS Coronavirus Main Proteinase]]<br />
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*[[SARS-CoV-2 Coronavirus Main Protease]]<br />
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*[[Taylor SARS-CoV2 Protease]]<br />
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== 3D Structures of Virus protease ==
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[[Virus protease 3D structures]]
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</StructureSection>
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==References==
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== 3D Structures of Virus proteases ==
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<references />
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[[Category:Topic Page]]
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===HIV-1===
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[[3ixo]] - HIV1-PR subtype A<br />
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[[1odx]], [[ 2hb2]], [[ 2hb4]], [[ 2pc0]] - HIV1-PR (mutant) <br />
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[[1rpi]], [[ 1rq9]], [[ 1tw7]] - HIV1-PR (drug-resistant mutant) <br />
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[[1odw]], [[ 3kf1]] - HIV1-PR
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===HIV-1 complexes===
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[[1hsg]], [[ 1hsh]], [[ 1hsi]], [[ 3oxc]], [[ 3ekv]], [[ 3ekx]], [[ 3eky]], [[ 3el1]], [[ 1ohr]] - HIV1-PR + antiviral drug<br />
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[[1aid]], [[ 1qbr]], [[ 1qbs]], [[ 1qbt]], [[ 1qbu]], [[ 3mxe]], [[ 3m9f ]], [[ 3kf0]], [[ 3kf1]], [[ 3kfn]], [[ 3kfp]], [[ 3kfr]], [[ 3kfs]], [[ 2wkz]], [[ 2wl0]], [[ 3gga]], [[ 3ggv]], [[ 3ggx]], [[ 2uxz]], [[ 2uy0]], [[ 1zp8]], [[ 1xl2]], [[ 1xl5]], [[ 1zpa]], [[ 1yt9]], [[ 2a4f ]], [[ 1upj]], [[ 2upj]], [[ 7upj]], [[ 1hxb]], [[ 1hih]], [[ 1hvr]], [[ 1hef]], [[ 1heg]], [[ 4phv]], [[ 1w5w]], [[ 1w5x]], [[ 1w5v]], [[ 1w5y]], [[ 1t7k]], [[ 1npa]], [[ 1npv]], [[ 1npw]], [[ 1eby]], [[ 1ec0]], [[ 1g2k]], [[ 1c6x]], [[ 1c6y]], [[ 1c6z]], [[ 1hwr]], [[ 2bpv]], [[ 2bpw]], [[ 2bpx]], [[ 2bpy]], [[ 2bpz]], [[ 1ody]], [[ 1hvh]], [[ 3tlh]], [[ 1hxw]] - HIV1-PR + inhibitor<br />
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[[2zye]] - HIV1-PR + inhibitor - neutron<br />
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3aid]], [[ 1ytg]], [[ 1yth]], [[ 2nxd]], [[ 2nxl]], [[ 2nxm]], [[ 2fns]], [[ 2fnt]], [[ 1zj7]], [[ 1zlf]], [[ 1zpk]], [[ 1zsf]], [[ 1zsr]], [[
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1cpi]], [[ 1m0b]], [[ 1iiq]], [[ 1fqx]], [[ 1a30]] - HIV1-PR + polypeptide derivative
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1sp5]] - HIV1-PR + autoproteolytic peptide
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===HIV-1 (mutant) complexes===
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[[3nu3]], [[ 3nu4]], [[ 3nu5]], [[ 3nu6]], [[ 3nu9]], [[ 3nuj]], [[ 3nuo]], [[ 2qhc]], [[ 2qak]], [[ 2pym]], [[ 2pyn]], [[ 2q63]], [[ 2q64]], [[ 2fxd]], [[ 2fxe]], [[ 2fgu]], [[ 2fgv]], [[ 1sdt]], [[ 1sdu]], [[ 1sdv]], [[ 1d4y]], [[ 1d4s]] - HIV1-PR (mutant) + antiviral drug<br />
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[[2aid]], [[ 1hpo]], [[ 1tcx]], [[ 1gnm]], [[ 1gnn]], [[ 1gno]], [[ 1kzk]], [[ 3ok9]], [[ 3i8w]], [[ 3i7e]], [[ 3bxr]], [[ 3bxs]], [[ 2hc0]], [[ 2psu]], [[ 2psv]], [[ 2fle]], [[ 2f3k]], [[ 2ien]], [[ 2fdd]], [[ 2fde]], [[ 1t7i]], [[ 1t3r]], [[ 1mrw]], [[ 1mrx]], [[ 1msm]], [[ 1msn]], [[ 1bv9]] - HIV1-PR (mutant) + inhibitor<br />
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[[2p3b]] - HIV1-PR subtype B (mutant) + inhibitor<br />
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[[2p3c]] - HIV1-PR subtype F (mutant) + inhibitor<br />
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[[1zbg]], [[ 1z8c]], [[ 2az9]], [[ 2azc]], [[ 2a1e]], [[ 1lzq]], [[ 1d4k]], [[ 1d4l]], [[ 1a8k]], [[ 1a94]], [[ 1axa]] - HIV1-PR (mutant) + polypeptide derivative<br />
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[[1ztz]] - HIV1-PR (mutant) + autoproteolytic polypeptide + metalacarborane
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===HIV-1 (drug-resistant mutant) complexes===
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[[3el4]], [[ 3el9]], [[ 3em3]], [[ 3em4]], [[ 3em6]], [[ 3ggt]], [[ 3ggu]], [[ 1t7j]], [[ 1rv7]], [[ 1n49]], [[ 1fb7]] - HIV1-PR (drug-resistant mutant) + antiviral drug<br />
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[[1izh]], [[ 1izi]], [[ 1fb7]] - HIV1-PR (drug-resistant mutant) + inhibitor<br />
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[[2p3a]] - HIV1-PR subtype B (drug-resistant mutant) + inhibitor<br />
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2p3d]] - HIV1-PR subtype F (drug-resistant mutant) + inhibitor<br />
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===HIV-2===
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[[1jld]] - HIV2-PR<br />
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[[1hii]] - HIV2-PR + inhibitor<br />
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[[5upj]], [[ 6upj]], [[ 3upj]], [[ 4upj]] - HIV2-PR (mutant) + inhibitor<br />
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[[1ida]], [[ 1idb]], [[ 2mip]] - HIV2-PR + polypeptide derivative
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===Feline Immunodeficiency Virus-PR===
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[[2hah]] - FIV-PR residues 39-154 (mutant) + inhibitor<br />
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[[5fiv]], [[ 6fiv]], [[ 1b11]] - FIV-PR + inhibitor<br />
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===Simian Immunodeficiency Virus-PR]]]
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[[2sam]] - SIV-PR + inhibitor<br />
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[[1az5]] - SIV-PR (mutant)
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===XMRV-PR===
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[[3nr6]] – XMRV-PR P14<br />
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[[3p1g]] – XMRV-PR RNase H domain (mutant)
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Current revision

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

Drag the structure with the mouse to rotate

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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