1v9u
From Proteopedia
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|PDB= 1v9u |SIZE=350|CAPTION= <scene name='initialview01'>1v9u</scene>, resolution 3.6Å | |PDB= 1v9u |SIZE=350|CAPTION= <scene name='initialview01'>1v9u</scene>, resolution 3.6Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1fpn|1FPN]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9u OCA], [http://www.ebi.ac.uk/pdbsum/1v9u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v9u RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously. | Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously. | ||
- | |||
- | ==Disease== | ||
- | Known disease associated with this structure: Cerebellar hypoplasia, VLDLR-associated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192977 192977]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Reithmayer, M.]] | [[Category: Reithmayer, M.]] | ||
[[Category: Verdaguer, N.]] | [[Category: Verdaguer, N.]] | ||
- | [[Category: CA]] | ||
- | [[Category: DAO]] | ||
[[Category: human rhinovirus]] | [[Category: human rhinovirus]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
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[[Category: vldl-receptor]] | [[Category: vldl-receptor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:21:28 2008'' |
Revision as of 21:21, 30 March 2008
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, resolution 3.6Å | |||||||
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Ligands: | , | ||||||
Related: | 1FPN
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Human Rhinovirus 2 bound to a fragment of its cellular receptor protein
Overview
Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously.
About this Structure
1V9U is a Protein complex structure of sequences from Homo sapiens and Human rhinovirus 2. Full crystallographic information is available from OCA.
Reference
X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein., Verdaguer N, Fita I, Reithmayer M, Moser R, Blaas D, Nat Struct Mol Biol. 2004 May;11(5):429-34. Epub 2004 Apr 4. PMID:15064754
Page seeded by OCA on Mon Mar 31 00:21:28 2008