1nob

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{{STRUCTURE_1nob| PDB=1nob | SCENE= }}
{{STRUCTURE_1nob| PDB=1nob | SCENE= }}
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'''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12'''
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===KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12===
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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: Zhang, Y B.]]
[[Category: Zhang, Y B.]]
[[Category: Receptor binding]]
[[Category: Receptor binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:46:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:43:23 2008''

Revision as of 10:43, 29 July 2008

Image:1nob.png

Template:STRUCTURE 1nob

KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12

Template:ABSTRACT PUBMED 10567268

About this Structure

1NOB is a Single protein structure of sequence from 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

Page seeded by OCA on Tue Jul 29 13:43:23 2008

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