[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1093/nar/13.6.2111; PubMed=2987843 [NCBI, ExPASy, EBI, Israel, Japan]
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. 13:2111-2126(1985).
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[2]
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SEQUENCE REVISION.
Kuechler E.;
Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
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[3]
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FUNCTION OF THE LEADER PROTEASE.
DOI=10.1016/S0014-5793(00)01928-1; PubMed=11034318 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser W.,
Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-239.
PubMed=1338980 [NCBI, ExPASy, EBI, Israel, Japan]
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. 1:1154-1161(1992).
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[5]
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X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 851-992.
DOI=10.1093/emboj/18.20.5463; PubMed=10523291 [NCBI, ExPASy, EBI, Israel, Japan]
Petersen J.F.,
Cherney M.M.,
Liebig H.D.,
Skern T.,
Kuechler E.,
James M.N.;
"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. 18:5463-5475(1999).
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[6]
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X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1508-1687.
DOI=10.1073/pnas.96.20.11000; PubMed=10500114 [NCBI, ExPASy, EBI, Israel, Japan]
Matthews D.A.,
Dragovich P.S.,
Webber S.E.,
Fuhrman S.A.,
Patick A.K.,
Zalman L.S.,
Hendrickson T.F.,
Love R.A.,
Prins T.J.,
Marakovits J.T.,
Zhou R.,
Tikhe J.,
Ford C.E.,
Meador J.W.,
Ferre R.A.,
Brown E.L.,
Binford S.L.,
Brothers M.A.,
DeLisle D.M.,
Worland S.T.;
"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. 96:11000-11007(1999).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 71-856.
DOI=10.1006/jmbi.2000.3943; PubMed=10903863 [NCBI, ExPASy, EBI, Israel, Japan]
Verdaguer N.,
Blaas D.,
Fita I.;
"Structure of human rhinovirus serotype 2 (HRV2).";
J. Mol. Biol. 300:1179-1194(2000).
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- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with human ICAM1 to provide virion attachment to target cell (By similarity).
- FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
- FUNCTION: Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription.
- FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
- FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).
- FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
- CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
- SUBUNIT: Capsid proteins interact with host ICAM1 (By similarity).
- SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
- SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).
- PTM: VPg is covalently linked to the genomic RNA (By similarity).
- PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
- SIMILARITY: Belongs to the picornaviruses polyprotein family.
- SIMILARITY: Contains 2 peptidase C3 domains [view classification].
- SIMILARITY: Contains 1 RdRp catalytic domain.
- SIMILARITY: Contains 1 SF3 helicase domain.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure associated with cellular receptor; URL="http://viperdb.scripps.edu/info_page.php?VDB=1fpn";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure complexed with cellular receptor fragment; URL="http://viperdb.scripps.edu/info_page.php?VDB=1v9u";.
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