1kac: Difference between revisions

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[[Image:1kac.~~gif~~|left|200px]]

[[Image:1kac.png|left|200px]]

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

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

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10567268}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10567268 is the PubMed ID number.

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==About this Structure==

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[[Category: Adhesion protein receptor complex]]

[[Category: Viral protein/receptor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:30:03 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:01:52 2008''

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-[[Image:1kac.gif|left|200px]]
+{{Seed}}
+[[Image:1kac.png|left|200px]]
 <!--
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 {{STRUCTURE_1kac|  PDB=1kac  |  SCENE=  }}
-'''KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR'''
+===KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10567268}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10567268 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10567268}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Adhesion protein receptor complex]]
 [[Category: Viral protein/receptor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:30:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:01:52 2008''