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SUMMARY:Structural studies of the human drug-metabolising protein CYP3A4
DTSTART;VALUE=DATE-TIME:20250922T161000Z
DTEND;VALUE=DATE-TIME:20250922T162000Z
DTSTAMP;VALUE=DATE-TIME:20260527T011025Z
UID:indico-contribution-1838@lindico453.srv.lu.se
DESCRIPTION:Speakers: Johan Glerup (University of Gothenburg)\nA highly fl
 exible protein with an active site that changes its volume to fit a wide v
 ariety of ligands. A lid made of loops changes conformation based on ligan
 d-size. Inhibition of this enzyme stops metabolism of drugs. This is an au
 tomatic disqualification of a drug candidate. Room temperature SSX shows b
 etter definition of some flexible loops\, even at worse resolution. SSX da
 ta collection at tens of kilo Gray produces a similar active-site to our X
 FEL structure. I present an internal distance matrix analysis of a subset 
 of PDB CYP3A4 structures to determine that crystal form\, resolution and t
 o some extent ligand-size dominates the clustering of global similarity wi
 th little difference caused by temperature. The protein crystalises as a m
 onomer in the ASU but SAX\, cryo-EM and SEC-MALS shows a homo-tetramer in 
 solution bringing it into the perfect size range for cryo-EM. I present in
 itial data for the volume of the tetramer solved through single particle a
 nalysis at SciLifeLab Solna.\n\n\nCo-authors: Owens Uwangue\, Gisela Brand
 en\, Monika Bjelcic\n\nhttps://lindico453.srv.lu.se/event/583/contribution
 s/1838/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1838/
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