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PDBsum entry 3dpr
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269 a.a.
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250 a.a.
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237 a.a.
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25 a.a.
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39 a.a.
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* Residue conservation analysis
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PDB id:
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Virus
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Title:
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Human rhinovirus 2 bound to a concatamer of the vldl receptor module v3
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Structure:
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Protein vp1. Chain: a. Synonym: virion protein 1, p1d, coat protein vp1. Protein vp2. Chain: b. Synonym: virion protein 2, p1b, coat protein vp2. Protein vp3. Chain: c. Synonym: virion protein 3, p1c, coat protein vp3.
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Source:
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Human rhinovirus 2. Hrv-2. Organism_taxid: 12130. Strain: human. Other_details: hela cells. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli.
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Resolution:
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3.50Å
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R-factor:
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0.426
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R-free:
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0.441
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Authors:
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J.Querol-Audi,J.Pous,I.Fita,N.Verdaguer
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Key ref:
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J.Querol-Audí
et al.
(2009).
Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition.
Febs Lett,
583,
235-240.
PubMed id:
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Date:
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09-Jul-08
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Release date:
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07-Apr-09
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PROCHECK
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Headers
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References
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P04936
(POLG_HRV2) -
Genome polyprotein from Human rhinovirus 2
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Seq:
Struc:
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2150 a.a.
269 a.a.
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P04936
(POLG_HRV2) -
Genome polyprotein from Human rhinovirus 2
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Seq:
Struc:
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2150 a.a.
250 a.a.
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P04936
(POLG_HRV2) -
Genome polyprotein from Human rhinovirus 2
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Seq:
Struc:
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2150 a.a.
237 a.a.
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Enzyme class 1:
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Chains A, B, C, D:
E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Enzyme class 2:
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Chains A, B, C, D:
E.C.3.4.22.28
- picornain 3C.
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Reaction:
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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.
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Enzyme class 3:
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Chains A, B, C, D:
E.C.3.4.22.29
- picornain 2A.
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Reaction:
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Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
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Enzyme class 4:
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Chains A, B, C, D:
E.C.3.6.1.15
- nucleoside-triphosphate phosphatase.
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Reaction:
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a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
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ribonucleoside 5'-triphosphate
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+
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H2O
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=
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ribonucleoside 5'-diphosphate
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+
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phosphate
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Febs Lett
583:235-240
(2009)
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PubMed id:
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Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition.
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J.Querol-Audí,
T.Konecsni,
J.Pous,
O.Carugo,
I.Fita,
N.Verdaguer,
D.Blaas.
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ABSTRACT
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X-ray structures of human rhinovirus 2 (HRV2) in complex with soluble
very-low-density lipoprotein receptors encompassing modules 1, 2, and 3 (V123)
and five V3 modules arranged in tandem (V33333) demonstrates multi-modular
binding around the virion's five-fold axes. Occupancy was 60% for V123 and 100%
for V33333 explaining the high-avidity of the interaction. Surface potentials of
3D-models of all minor group HRVs and K-type major group HRVs were compared;
hydrophobic interactions between a conserved lysine in the viruses and a
tryptophan in the receptor modules together with coulombic attraction via
diffuse opposite surface potentials determine minor group HRV receptor
specificity.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.Fuchs,
and
D.Blaas
(2010).
Uncoating of human rhinoviruses.
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Rev Med Virol,
20,
281-297.
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T.J.Tuthill,
E.Groppelli,
J.M.Hogle,
and
D.J.Rowlands
(2010).
Picornaviruses.
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Curr Top Microbiol Immunol,
343,
43-89.
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D.Beglov,
C.J.Lee,
A.De Biasio,
D.Kozakov,
R.Brenke,
S.Vajda,
and
N.Beglova
(2009).
Structural insights into recognition of beta2-glycoprotein I by the lipoprotein receptors.
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Proteins,
77,
940-949.
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T.Konecsni,
U.Berka,
A.Pickl-Herk,
G.Bilek,
A.G.Khan,
L.Gajdzig,
R.Fuchs,
and
D.Blaas
(2009).
Low pH-triggered beta-propeller switch of the low-density lipoprotein receptor assists rhinovirus infection.
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J Virol,
83,
10922-10930.
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V.U.Weiss,
G.Bilek,
A.Pickl-Herk,
D.Blaas,
and
E.Kenndler
(2009).
Mimicking virus attachment to host cells employing liposomes: analysis by chip electrophoresis.
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Electrophoresis,
30,
2123-2128.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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