1kac: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1nob|1NOB]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kac OCA], [http://www.ebi.ac.uk/pdbsum/1kac PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kac RCSB]</span> | |||
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==Overview== | ==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. | 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== | ||
1KAC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/ | 1KAC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_adenovirus_12 Human adenovirus 12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAC 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://www.ncbi.nlm.nih.gov/pubmed/10567268 10567268] | 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: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human adenovirus | [[Category: Human adenovirus 12]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bewley, M C.]] | [[Category: Bewley, M C.]] | ||
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[[Category: viral protein/receptor complex]] | [[Category: viral protein/receptor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:39 2008'' | ||
Revision as of 21:45, 30 March 2008
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| , resolution 2.6Å | |||||||
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| Related: | 1NOB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR
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
1KAC is a Protein complex structure of sequences from Homo sapiens and Human adenovirus 12. 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
Page seeded by OCA on Sun Mar 30 21:45:39 2008