1kac

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{{STRUCTURE_1kac| PDB=1kac | SCENE= }}
{{STRUCTURE_1kac| PDB=1kac | SCENE= }}
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'''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR'''
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===KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10567268 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10567268}}
==About this Structure==
==About this Structure==
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[[Category: Adhesion protein receptor complex]]
[[Category: Adhesion protein receptor complex]]
[[Category: Viral protein/receptor complex]]
[[Category: Viral protein/receptor complex]]
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Revision as of 07:01, 2 July 2008

Image:1kac.png

Template:STRUCTURE 1kac

KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR

Template:ABSTRACT PUBMED 10567268

About this Structure

1KAC is a Protein complex structure of sequences from Homo sapiens and Human adenovirus 12. Full crystallographic information is available from OCA.

Reference

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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