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- PDB-1v9u: Human Rhinovirus 2 bound to a fragment of its cellular receptor p... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1v9u | ||||||
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Title | Human Rhinovirus 2 bound to a fragment of its cellular receptor protein | ||||||
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![]() | Virus/Receptor / human rhinovirus / VLDL-receptor / virus-protein complex / Icosahedral virus / Virus-Receptor COMPLEX | ||||||
Function / homology | ![]() reelin receptor activity / VLDL clearance / glycoprotein transport / ventral spinal cord development / very-low-density lipoprotein particle receptor activity / Reelin signalling pathway / very-low-density lipoprotein particle binding / reelin-mediated signaling pathway / low-density lipoprotein particle receptor activity / very-low-density lipoprotein particle clearance ...reelin receptor activity / VLDL clearance / glycoprotein transport / ventral spinal cord development / very-low-density lipoprotein particle receptor activity / Reelin signalling pathway / very-low-density lipoprotein particle binding / reelin-mediated signaling pathway / low-density lipoprotein particle receptor activity / very-low-density lipoprotein particle clearance / very-low-density lipoprotein particle / positive regulation of dendrite development / lipid transport / dendrite morphogenesis / cargo receptor activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / apolipoprotein binding / clathrin-coated pit / picornain 2A / VLDLR internalisation and degradation / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / symbiont genome entry into host cell via pore formation in plasma membrane / cholesterol metabolic process / picornain 3C / receptor-mediated endocytosis / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / memory / calcium-dependent protein binding / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / nervous system development / symbiont-mediated suppression of host gene expression / DNA replication / RNA helicase activity / receptor complex / induction by virus of host autophagy / RNA-directed RNA polymerase / lysosomal membrane / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / calcium ion binding / host cell nucleus / virion attachment to host cell / structural molecule activity / signal transduction / proteolysis / RNA binding / ATP binding / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Verdaguer, N. / Fita, I. / Reithmayer, M. / Moser, R. / Blaas, D. | ||||||
![]() | ![]() Title: X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein Authors: Verdaguer, N. / Fita, I. / Reithmayer, M. / Moser, R. / Blaas, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 178.9 KB | Display | ![]() |
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PDB format | ![]() | 138.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 411 KB | Display | ![]() |
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Full document | ![]() | 463.4 KB | Display | |
Data in XML | ![]() | 24.4 KB | Display | |
Data in CIF | ![]() | 36 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fpnS S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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