1nob
From Proteopedia
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| - | [[Image:1nob.gif|left|200px]] | + | [[Image:1nob.gif|left|200px]] |
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| - | '''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12''' | + | {{Structure |
| + | |PDB= 1nob |SIZE=350|CAPTION= <scene name='initialview01'>1nob</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NOB is a [ | + | 1NOB is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10567268 10567268] |
[[Category: Human adenovirus 37]] | [[Category: Human adenovirus 37]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor binding]] | [[Category: receptor binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:59:30 2008'' |
Revision as of 10:59, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12
Overview
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
1NOB is a Single protein structure of sequence from Human adenovirus 37. 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 Thu Mar 20 12:59:30 2008
