1v9u

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(New page: 200px<br /> <applet load="1v9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v9u, resolution 3.6&Aring;" /> '''Human Rhinovirus 2 b...)
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[[Image:1v9u.gif|left|200px]]<br />
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[[Image:1v9u.gif|left|200px]]<br /><applet load="1v9u" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1v9u" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1v9u, resolution 3.6&Aring;" />
caption="1v9u, resolution 3.6&Aring;" />
'''Human Rhinovirus 2 bound to a fragment of its cellular receptor protein'''<br />
'''Human Rhinovirus 2 bound to a fragment of its cellular receptor protein'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1V9U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with CA and DAO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V9U OCA].
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1V9U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DAO:'>DAO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9U OCA].
==Reference==
==Reference==
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[[Category: vldl-receptor]]
[[Category: vldl-receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:42:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:13 2008''

Revision as of 13:33, 21 February 2008


1v9u, resolution 3.6Å

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Human Rhinovirus 2 bound to a fragment of its cellular receptor protein

Contents

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.

Disease

Known disease associated with this structure: Cerebellar hypoplasia, VLDLR-associated OMIM:[192977]

About this Structure

1V9U is a Protein complex structure of sequences from Homo sapiens and Human rhinovirus 2 with and as ligands. 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

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