1nob

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Revision as of 23:18, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1nob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nob, resolution 2.6Å" /> '''KNOB DOMAIN FROM ADEN...)
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File:1nob.gif


1nob, resolution 2.6Å

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KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12

OverviewOverview

Binding of virus particles to specific host cell surface receptors is, known to be an obligatory step in infection even though the molecular, basis for these interactions is not well characterized. The crystal, structure of the adenovirus fiber knob domain in complex with domain I of, its human cellular receptor, coxsackie and adenovirus receptor (CAR), is, presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting, surfaces create interfacial solvent-filled cavities and channels that may, be targets for antiviral drug therapy. The structure identifies key, determinants of binding specificity, which may suggest ways to modify the, tropism of adenovirus-based gene therapy vectors.

About this StructureAbout this Structure

1NOB is a Single protein structure of sequence from Human adenovirus 37. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR., Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM, Science. 1999 Nov 19;286(5444):1579-83. PMID:10567268

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