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1h8t

From Proteopedia

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{{STRUCTURE_1h8t| PDB=1h8t | SCENE= }}
{{STRUCTURE_1h8t| PDB=1h8t | SCENE= }}
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'''ECHOVIRUS 11'''
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===ECHOVIRUS 11===
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==Overview==
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We have used X-ray crystallography to determine the structure of a decay accelerating factor (DAF)-binding, clinic-derived isolate of echovirus 11 (EV11-207). The structures of the capsid proteins closely resemble those of capsid proteins of other picornaviruses. The structure allows us to interpret a series of amino acid changes produced by passaging EV11-207 in different cell lines as highlighting the locations of multiple receptor-binding sites on the virion surface. We suggest that a DAF-binding site is located at the fivefold axes of the virion, while the binding site for a distinct but as yet unidentified receptor is located within the canyon surrounding the virion fivefold axes.
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The line below this paragraph, {{ABSTRACT_PUBMED_12097583}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12097583 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12097583}}
==About this Structure==
==About this Structure==
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[[Category: Echovirus]]
[[Category: Echovirus]]
[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:34:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:49:55 2008''

Revision as of 03:49, 1 July 2008

Image:1h8t.png

Template:STRUCTURE 1h8t

ECHOVIRUS 11

Template:ABSTRACT PUBMED 12097583

About this Structure

1H8T is a Protein complex structure of sequences from Human echovirus 11. Full crystallographic information is available from OCA.

Reference

Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection., Stuart AD, McKee TA, Williams PA, Harley C, Shen S, Stuart DI, Brown TD, Lea SM, J Virol. 2002 Aug;76(15):7694-704. PMID:12097583

Page seeded by OCA on Tue Jul 1 06:49:55 2008

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