Genome polyprotein
Details
- Name
- Genome polyprotein
- Synonyms
- 3.4.22.29
- P2A
- Gene Name
- Not Available
- Organism
- HRV-2
- Amino acid sequence
>lcl|BSEQ0019129|Genome polyprotein MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASNGASKLEFTQDPSKFTDPVKDV LEKGIPTLQSPTVEACGYSDRIIQITRGDSTITSQDVANAIVAYGVWPHYLSSKDASAID KPSQPDTSSNRFYTLRSVTWSSSSKGWWWKLPDALKDMGIFGENMFYHYLGRSGYTIHVQ CNASKFHQGTLIVALIPEHQIASALHGNVNVGYNYTHPGETGREVKAETRLNPDLQPTEE YWLNFDGTLLGNITIFPHQFINLRSNNSATIIAPYVNAVPMDSMRSHNNWSLVIIPICPL ETSSAINTIPITISISPMCAEFSGARAKRQGLPVFITPGSGQFLTTDDFQSPCALPWYHP TKEISIPGEVKNLVEICQVDSLVPINNTDTYINSENMYSVVLQSSINAPDKIFSIRTDVA SQPLATTLIGEISSYFTHWTGSLRFSFMFCGTANTTVKLLLAYTPPGIAEPTTRKDAMLG THVIWDVGLQSTISMVVPWISASHYRNTSPGRSTSGYITCWYQTRLVIPPQTPPTARLLC FVSGCKDFCLRMARDTNLHLQSGAIAQNPVENYIDEVLNEVLVVPNINSSNPTTSNSAPA LDAAETGHTSSVQPEDVIETRYVQTSQTRDEMSLESFLGRSGCIHESKLEVTLANYNKEN FTVWAINLQEMAQIRRKFELFTYTRFDSEITLVPCISALSQDIGHITMQYMYVPPGAPVP NSRDDYAWQSGTNASVFWQHGQAYPRFSLPFLSVASAYYMFYDGYDEQDQNYGTANTNNM GSLCSRIVTEKHIHKVHIMTRIYHKAKHVKAWCPRPPRALEYTRAHRTNFKIEDRSIQTA IVTRPIITTAGPSDMYVHVGNLIYRNLHLFNSEMHESILVSYSSDLIIYRTNTVGDDYIP SCDCTQATYYCKHKNRYFPITVTSHDWYEIQESEYYPKHIQYNLLIGEGPCEPGDCGGKL LCKHGVIGIVTAGGDNHVAFIDLRHFHCAEEQGVTDYIHMLGEAFGNGFVDSVKEHIHAI NPVGNISKKIIKWMLRIISAMVIIIRNSSDPQTILATLTLIGCSGSPWRFLKEKFCKWTQ LNYIHKESDSWLKKFTEACNAARGLEWIGNKISKFIEWMKSMLPQAQLKVKYLNELKKLN LYEKQVESLRVADMKTQEKIKMEIDTLHDLSRKFLPLYASEAKRIKTLYIKCDNIIKQKK RCEPVAIVIHGPPGAGKSITTNFLAKMITNDSDIYSLPPDPKYFDGYDQQSVVIMDDIMQ NPAGDDMTLFCQMVSSVTFIPPMADLPDKGKAFDSRFVLCSTNHSLLTPPTITSLPAMNR RFFLDLDIIVHDNFKDPQGKLNVAAAFRPCDVDNRIGNARCCPFVCGKAVSFKDRNSCNK YSLAQVYNIMIEEDRRRRQVVDVMTAIFQGPIDMKNPPPPAITDLLQSVRTPEVIKYCEG NRWIIPAECKIEKELNLANTIITIIANVIGMARIIYVIYKLFCTLQGPYSGEPKPKTKIP ERRVVTQGPEEEFGMSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGIT TKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNNEDDYPNCNLALLANQPEPTI INVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAM LLRSYFTDVQGQITLSKKTSECNLPSIHTPCKTKLQPSVFYDVFPGSKEPAVLSEKDARL QVDFNEALFSKYKGNTDCSINDHIRIASSHYAAQLITLDIDPKPITLEDSVFGTDGLEAL DLNTSAGFPYIAMGVKKRDLINNKTKDISKLKEAIDKYGVDLPMVTFLKDELRKHEKVIK GKTRVIEASSVNDTLLFRTTFGNLFSKFHLNPGIVTGSAVGCDPEVFWSKIPAMLDDKCI MAFDYTNYDGSIHPIWFEALKQVLVDLSFNPTLIDRLCKSKHIFKNTYYEVEGGVPSGCS GTSIFNTMINNIIIRTLVLDAYKNIDLDKLKIIAYGDDVIFSYIHELDMEAIAIEGVKYG LTITPADKSNTFVKLDYSNVTFLKRGFKQDEKYNFLIHPTFPEDEIFESIRWTKKPSQMH EHVLSLCHLMWHNGRDAYKKFVEKIRSVSAGRALYIPPYDLLLHEWYEKF
- Number of residues
- 2150
- Molecular Weight
- 241975.505
- Theoretical pI
- 7.23
- GO Classification
- FunctionsATP binding / cysteine-type endopeptidase activity / ion channel activity / RNA binding / RNA helicase activity / RNA-directed RNA polymerase activity / structural molecule activityProcessesDNA replication / endocytosis involved in viral entry into host cell / induction by virus of host autophagy / pore formation by virus in membrane of host cell / pore-mediated entry of viral genome into host cell / positive stranded viral RNA replication / protein oligomerization / RNA-protein covalent cross-linking / suppression by virus of host gene expression / suppression by virus of host mRNA export from nucleus / suppression by virus of host RIG-I activity by RIG-I proteolysis / suppression by virus of host translation initiation factor activity / transcription, DNA-templated / viral RNA genome replication / virion attachment to host cellComponentshost cell cytoplasmic vesicle membrane / integral to membrane of host cell / membrane / T=pseudo3 icosahedral viral capsid
- General Function
- Structural molecule activity
- Specific Function
- Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host VLDLR to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0002965|6453 bp ATGGGTGCACAGGTTTCAAGACAAAATGTTGGAACTCACTCCACGCAAAACTCTGTATCA AATGGGTCTAGTTTAAATTATTTTAACATCAATTATTTCAAAGATGCTGCTTCAAATGGT GCATCAAAACTGGAATTCACACAAGATCCTAGTAAATTTACTGACCCAGTTAAGGATGTT TTGGAAAAGGGAATACCAACACTACAGTCCCCCACAGTGGAGGCTTGTGGATACTCTGAT AGGATTATACAGATTACCAGAGGAGATTCAACCATAACCTCACAAGATGTGGCTAATGCT ATCGTTGCGTATGGTGTTTGGCCACATTATCTATCCTCCAAGGATGCCTCTGCAATTGAT AAACCCTCTCAACCAGATACATCTTCTAATAGATTTTATACTCTAAGGAGTGTGACCTGG AGCAGTTCCTCAAAGGGTTGGTGGTGGAAACTACCTGATGCACTCAAGGACATGGGTATT TTTGGTGAAAACATGTTTTATCATTACCTGGGTAGGAGTGGATACACAATACATGTGCAG TGTAATGCTAGTAAATTTCACCAGGGTACACTAATTGTTGCTCTGATACCTGAGCATCAG ATTGCAAGTGCCTTACATGGCAATGTGAATGTTGGTTACAACTACACACACCCAGGTGAA ACAGGCAGGGAAGTTAAAGCTGAGACGAGATTGAATCCTGATCTACAACCTACTGAAGAG TATTGGCTAAACTTTGATGGGACACTCCTTGGAAATATTACCATATTCCCTCATCAATTT ATCAACTTGAGGAGTAATAATTCTGCCACAATAATTGCCCCTTATGTCAATGCAGTTCCT ATGGATTCAATGCGGAGCCACAATAATTGGAGTTTGGTAATAATACCAATATGTCCCCTT GAGACATCAAGTGCAATTAACACAATACCTATTACAATATCTATAAGCCCCATGTGTGCA GAGTTTTCCGGCGCGCGTGCCAAGCGTCAAGGATTACCAGTTTTCATCACACCAGGTTCA GGACAGTTTTTGACAACAGATGATTTCCAATCCCCATGTGCACTTCCCTGGTATCACCCA ACTAAGGAAATTTCTATTCCAGGTGAGGTTAAAAATTTGGTTGAAATTTGTCAAGTAGAC AGCCTAGTACCAATAAATAACACTGACACCTACATCAATAGTGAAAATATGTATTCTGTT GTATTGCAATCATCAATTAATGCACCAGATAAGATCTTCTCTATTCGAACAGATGTTGCT TCCCAACCTTTAGCTACTACTTTGATTGGTGAGATATCTAGCTATTTCACCCACTGGACA GGGAGTCTCCGTTTCAGCTTCATGTTTTGTGGTACTGCCAACACTACTGTTAAGCTTTTG TTGGCATACACACCACCTGGTATCGCAGAACCCACCACAAGAAAGGATGCAATGCTAGGC ACTCATGTTATATGGGATGTGGGGTTGCAGTCTACAATATCAATGGTAGTGCCATGGATT AGCGCTAGTCATTATAGAAACACATCACCAGGTAGATCTACATCTGGGTACATAACATGC TGGTATCAGACTAGATTAGTCATTCCACCTCAGACCCCACCAACAGCTAGATTGTTATGT TTTGTATCTGGGTGCAAAGACTTTTGCTTGCGCATGGCACGAGATACTAACCTACACCTG CAAAGTGGTGCAATAGCACAGAACCCTGTTGAGAATTATATAGATGAAGTTCTTAATGAA GTTTTAGTTGTCCCAAATATTAATAGTAGTAACCCCACAACATCAAATTCTGCCCCAGCA TTAGATGCTGCAGAAACAGGGCACACTAGTAGTGTTCAACCAGAGGATGTCATTGAAACT AGGTATGTGCAGACATCACAAACAAGAGATGAAATGAGTTTAGAGAGTTTTCTTGGCAGA TCAGGATGCATACATGAATCTAAATTAGAGGTTACACTTGCAAATTATAACAAGGAGAAT TTTACAGTGTGGGCTATTAATCTACAAGAAATGGCTCAAATTAGAAGGAAATTTGAATTG TTCACCTATACTAGGTTTGATTCTGAAATAACCCTAGTTCCATGCATTTCCGCCCTTAGT CAGGACATTGGACACATCACAATGCAATACATGTATGTTCCACCAGGTGCACCGGTGCCC AATAGTAGGGACGATTATGCATGGCAGTCTGGCACTAATGCCTCTGTTTTCTGGCAACAT GGACAGGCTTATCCAAGATTTTCCTTACCTTTCCTAAGTGTGGCATCTGCTTATTACATG TTTTATGATGGGTATGATGAACAAGATCAAAACTATGGTACAGCAAACACAAATAACATG GGGTCACTATGCTCTAGGATAGTAACAGAGAAACACATTCATAAAGTACATATAATGACA AGAATCTATCACAAGGCTAAACATGTCAAGGCATGGTGTCCACGCCCACCCAGAGCGCTT GAGTATACTCGTGCTCATCGCACTAATTTTAAAATTGAGGATAGGAGTATTCAGACAGCA ATTGTGACCAGACCAATTATCACTACAGCTGGCCCCAGTGACATGTATGTTCATGTAGGT AACCTTATTTATAGAAATCTTCATCTTTTCAACTCTGAGATGCATGAATCTATTTTGGTA TCTTATTCATCAGATTTAATCATTTACCGAACAAACACTGTAGGTGATGATTACATTCCC TCTTGTGATTGTACCCAAGCTACTTATTATTGCAAACATAAAAATAGATACTTCCCAATT ACAGTTACAAGCCATGACTGGTATGAAATACAGGAAAGTGAGTACTATCCCAAACACATA CAGTACAATTTGTTGATTGGTGAGGGCCCTTGTGAACCAGGTGACTGTGGTGGAAAGTTG CTATGCAAACATGGTGTCATAGGTATAGTAACAGCTGGTGGTGATAATCATGTGGCTTTT ATTGACCTTAGACACTTCCATTGTGCTGAAGAACAAGGGGTTACAGATTATATACATATG CTAGGAGAAGCATTTGGAAATGGATTTGTGGATAGTGTAAAAGAACATATACATGCCATA AACCCAGTAGGAAATATCAGCAAGAAAATTATTAAATGGATGTTGAGAATAATATCAGCA ATGGTCATAATAATTAGAAACTCTTCTGACCCCCAAACTATATTAGCAACACTCACACTG ATTGGGTGTTCTGGATCACCCTGGAGATTTTTAAAGGAAAAATTCTGTAAATGGACACAG CTTAATTATATACACAAAGAATCAGATTCATGGTTAAAGAAATTTACTGAAGCATGCAAT GCAGCTAGAGGGCTTGAATGGATAGGGAATAAGATATCTAAATTTATTGAATGGATGAAG TCGATGCTCCCGCAAGCTCAATTGAAGGTTAAGTACTTAAACGAGCTTAAAAAACTCAAC CTATACGAAAAGCAAGTTGAGAGCTTGCGGGTGGCTGACATGAAAACACAAGAAAAAATT AAAATGGAAATAGACACTTTACATGATTTGTCACGTAAATTTCTACCTTTGTATGCAAGT GAGGCAAAAAGGATAAAAACCCTATACATTAAATGTGATAATATCATCAAGCAGAAGAAA AGATGTGAACCAGTAGCTATAGTTATTCATGGACCACCTGGTGCTGGCAAATCTATAACA ACAAATTTCCTGGCCAAAATGATAACTAATGATAGTGACATATACTCTCTACCTCCTGAT CCAAAATATTTTGATGGTTATGACCAACAGAGTGTAGTAATAATGGATGACATTATGCAG AATCCAGCCGGGGATGACATGACACTGTTCTGCCAAATGGTTTCTAGTGTTACATTTATA CCACCAATGGCTGATCTACCAGATAAAGGCAAGGCTTTTGATTCTAGGTTTGTATTATGC AGCACAAATCATTCCCTTCTAACACCCCCGACAATAACTTCACTACCTGCAATGAATAGA AGATTTTTCCTAGATTTAGATATAATAGTACATGATAACTTCAAAGATCCACAGGGCAAA CTTAATGTGGCAGCAGCGTTTCGACCATGTGATGTAGATAATAGAATAGGAAATGCACGT TGTTGTCCATTTGTGTGTGGAAAAGCAGTTTCTTTCAAAGATCGTAACTCTTGCAACAAA TACAGCCTTGCGCAGGTGTACAACATAATGATTGAAGAAGACAGACGGAGAAGACAAGTG GTTGATGTCATGACAGCTATATTCCAAGGGCCAATTGATATGAAAAACCCACCACCACCT GCTATTACTGACTTGCTCCAGTCTGTTAGAACCCCTGAAGTTATTAAGTATTGTGAGGGT AATAGATGGATAATTCCAGCAGAATGCAAGATAGAAAAGGAGTTGAACTTGGCTAACACA ATCATAACAATCATTGCAAATGTTATTGGTATGGCGAGAATAATATATGTTATTTACAAA CTTTTTTGCACATTACAGGGACCATATTCAGGAGAACCAAAGCCCAAGACTAAAATCCCA GAAAGGCGTGTAGTAACACAGGGACCAGAGGAGGAATTTGGGATGTCTTTAATTAAACAT AACTCATGTGTTATTACAACAGAAAATGGGAAATTCACAGGTCTTGGAGTATACGACAGA TTTGTGGTCGTACCAACACATGCAGATCCTGGAAAGGAAATTCAGGTTGATGGTATAACT ACAAAAGTCATTGACTCATATGACCTATACAACAAGAATGGGATAAAGCTAGAAATAACA GTACTTAAATTAGATAGAAATGAAAAATTTAGAGATATCAGGAGATATATACCTAACAAT GAAGATGATTACCCCAATTGCAACTTAGCACTGCTAGCAAACCAGCCTGAACCAACTATA ATCAATGTTGGAGATGTTGTATCCTATGGCAATATACTGCTCAGTGGCAACCAAACGGCT AGAATGCTTAAATACAGTTACCCAACTAAATCTGGTTACTGTGGAGGTGTCTTATACAAA ATTGGGCAAGTGCTTGGAATACATGTTGGGGGCAATGGTAGGGATGGTTTCTCAGCTATG TTACTCAGATCCTATTTCACTGATGTTCAGGGCCAAATAACGTTATCAAAGAAGACCAGT GAATGTAACCTACCCAGTATACACACCCCATGCAAAACCAAATTGCAGCCTAGTGTTTTC TATGATGTATTCCCTGGTTCAAAAGAACCAGCTGTGTTGTCTGAAAAAGATGCCCGGTTA CAAGTTGATTTCAATGAAGCACTATTTTCTAAATACAAAGGGAATACAGATTGCTCCATT AATGACCACATAAGAATTGCATCATCACATTATGCAGCACAACTCATTACCTTAGATATT GACCCAAAACCTATTACACTTGAGGACAGTGTCTTTGGCACTGATGGATTAGAGGCTCTT GATTTGAACACTAGCGCAGGATTTCCATATATTGCAATGGGAGTTAAAAAGAGAGATTTA ATAAACAACAAGACCAAGGATATAAGCAAACTTAAAGAAGCAATTGACAAATACGGAGTT GACTTACCTATGGTCACCTTCTTGAAAGATGAACTCAGAAAGCATGAAAAGGTAATTAAA GGTAAAACTAGAGTTATTGAAGCTAGTAGTGTGAATGATACCCTATTATTTAGAACAACT TTTGGCAACCTCTTTTCAAAGTTCCACTTGAATCCTGGAATTGTTACTGGATCAGCAGTT GGATGTGATCCAGAGGTGTTTTGGTCAAAAATACCAGCAATGTTGGATGATAAATGTATT ATGGCTTTTGATTATACAAATTATGATGGTAGTATACACCCTATTTGGTTTGAAGCTCTT AAACAGGTACTGGTAGATCTATCATTTAATCCAACATTAATAGATAGACTATGCAAGTCT AAACACATCTTCAAAAATACATACTATGAAGTGGAGGGAGGTGTACCATCTGGGTGTTCA GGTACTAGTATTTTTAACACTATGATCAATAATATTATCATAAGGACCTTAGTGTTAGAT GCATACAAGAATATAGATCTAGATAAGCTTAAGATAATTGCCTATGGTGATGATGTCATA TTCTCATACATACATGAACTGGACATGGAGGCTATAGCAATAGAGGGTGTTAAATATGGT TTGACTATAACTCCTGCTGATAAATCTAACACATTTGTAAAATTAGACTATAGCAATGTT ACTTTTTTAAAAAGAGGGTTTAAGCAAGATGAGAAGTATAACTTTCTAATACATCCAACT TTCCCTGAAGATGAAATATTTGAATCCATCAGATGGACAAAGAAACCATCACAAATGCAT GAACATGTGTTGTCTCTGTGTCACTTAATGTGGCACAATGGACGTGACGCATACAAAAAA TTTGTGGAGAAGATACGCAGTGTAAGCGCTGGTCGTGCACTGTACATCCCTCCGTATGAT TTGCTTTTGCATGAGTGGTATGAAAAATTTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P04936 UniProtKB Entry Name POLG_HRV2 GenBank Protein ID 1617204 GenBank Gene ID X02316 - General References
- Skern T, Sommergruber W, Blaas D, Gruendler P, Fraundorfer F, Pieler C, Fogy I, Kuechler E: Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region. Nucleic Acids Res. 1985 Mar 25;13(6):2111-26. [Article]
- Glaser W, Skern T: Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro. FEBS Lett. 2000 Sep 1;480(2-3):151-5. [Article]
- Hewat EA, Neumann E, Blaas D: The concerted conformational changes during human rhinovirus 2 uncoating. Mol Cell. 2002 Aug;10(2):317-26. [Article]
- Park N, Skern T, Gustin KE: Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. J Biol Chem. 2010 Sep 10;285(37):28796-805. doi: 10.1074/jbc.M110.143404. Epub 2010 Jul 9. [Article]
- Fuchs R, Blaas D: Uncoating of human rhinoviruses. Rev Med Virol. 2010 Sep;20(5):281-97. doi: 10.1002/rmv.654. [Article]
- Fuchs R, Blaas D: Productive entry pathways of human rhinoviruses. Adv Virol. 2012;2012:826301. doi: 10.1155/2012/826301. Epub 2012 Nov 26. [Article]
- Tormo J, Stadler E, Skern T, Auer H, Kanzler O, Betzel C, Blaas D, Fita I: Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2. Protein Sci. 1992 Sep;1(9):1154-61. [Article]
- Petersen JF, Cherney MM, Liebig HD, Skern T, Kuechler E, James MN: The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis. EMBO J. 1999 Oct 15;18(20):5463-75. [Article]
- 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. [Article]
- Verdaguer N, Blaas D, Fita I: Structure of human rhinovirus serotype 2 (HRV2). J Mol Biol. 2000 Jul 28;300(5):1179-94. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02313 Ethyl (4R)-4-{[(2R,5S)-2-(4-fluorobenzyl)-6-methyl-5-{[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino}-4-oxoheptanoyl]amino}-5-[(3S)-2-oxo-3-pyrrolidinyl]pentanoate experimental unknown Details DB03017 Lauric acid approved, experimental unknown Details