1nob: Difference between revisions
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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[[Image:1nob.gif|left|200px]]<br /><applet load="1nob" size=" | [[Image:1nob.gif|left|200px]]<br /><applet load="1nob" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nob, resolution 2.6Å" /> | caption="1nob, resolution 2.6Å" /> | ||
'''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12'''<br /> | '''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12'''<br /> | ||
==Overview== | ==Overview== | ||
Binding of virus particles to specific host cell surface receptors is | 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 Structure== | ==About this Structure== | ||
1NOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_37 Human adenovirus 37]. Full crystallographic information is available from [http:// | 1NOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_37 Human adenovirus 37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Human adenovirus 37]] | [[Category: Human adenovirus 37]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bewley, M | [[Category: Bewley, M C.]] | ||
[[Category: Flanagan, J | [[Category: Flanagan, J M.]] | ||
[[Category: Freimuth, P.]] | [[Category: Freimuth, P.]] | ||
[[Category: Springer, K.]] | [[Category: Springer, K.]] | ||
[[Category: Zhang, Y | [[Category: Zhang, Y B.]] | ||
[[Category: receptor binding]] | [[Category: receptor binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:12 2008'' | ||
Revision as of 15:08, 21 February 2008
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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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