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SUMMARY:Structural basis of coronavirus E protein interactions with human 
 PALS1 PDZ domain
DTSTART;VALUE=DATE-TIME:20211125T070100Z
DTEND;VALUE=DATE-TIME:20211125T070200Z
DTSTAMP;VALUE=DATE-TIME:20260306T090900Z
UID:indico-contribution-4218@events01.synchrotron.org.au
DESCRIPTION:Speakers: Airah Javorsky (La Trobe University)\nSARS-CoV-2 inf
 ection leads to coronavirus disease 2019 (COVID-19)\, which is associated 
 with severe and life-threatening pneumonia and respiratory failure. Howeve
 r\, the molecular basis of these symptoms remains unclear. SARS-CoV-1 E pr
 otein interferes with control of cell polarity and cell-cell junction inte
 grity in human epithelial cells by binding to the PALS1 PDZ domain\, a key
  component of the Crumbs polarity complex. We show that C-terminal PDZ bin
 ding motifs of SARS-CoV-1 and SARS-CoV-2 E proteins bind the PALS1 PDZ dom
 ain with 29.6 and 22.8 μM affinity\, whereas the related sequence from ME
 RS-CoV did not bind. We then determined crystal structures of PALS1 PDZ do
 main bound to both SARS-CoV-1 and SARS-CoV-2 E protein PDZ binding motifs.
  Our findings establish the structural basis for SARS-CoV-1/2 mediated sub
 version of Crumbs polarity signalling and serve as a platform for the deve
 lopment of small molecule inhibitors to suppress SARS-CoV-1/2 mediated dis
 ruption of polarity signalling in epithelial cells.\n\nhttps://events01.sy
 nchrotron.org.au/event/146/contributions/4218/
LOCATION:Online
URL:https://events01.synchrotron.org.au/event/146/contributions/4218/
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