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SUMMARY:Keynote 1\, Prof. Poul Nissen: Structure and Dynamics of Membrane 
 Transport Proteins
DTSTART;VALUE=DATE-TIME:20191009T111500Z
DTEND;VALUE=DATE-TIME:20191009T115500Z
DTSTAMP;VALUE=DATE-TIME:20260526T135934Z
UID:indico-contribution-752@lindico453.srv.lu.se
DESCRIPTION:Speakers: Poul Nissen (Aarhus University)\nUsing membrane prot
 ein crystallography\, small-angle scattering techniques\, and cryo-EM\, an
 d also a range of biochemical and biophysical methods such as electrophysi
 ology\, single-molecule FRET\, and molecular dynamics simulations\, we hav
 e obtained deep insight into the functional cycle of primary active transp
 orters of the P-type ATPase family. These transport ATPases are fundamenta
 l to physiology\, and malfunctions are linked to diseases such as neurolog
 ical and cardiovascular disorders. \nThe transmembrane gradients for the k
 ey cations Na+\, K+\, and Ca2+ are generated by Na+\,K+-ATPase and Ca2+-AT
 Pases. In brain\, Na+\,K+-ATPase activity accounts for an estimated 40-70%
  of total ATP hydrolysis and potentiates e.g. Na+ and K+ channels for thei
 r activity in action potentials\, membrane potential\, and Na+ coupled tra
 nsport of e.g. glucose\, metabolite\, neurotransmitters\, Ca2+ efflux\, pH
  and Cl- control. Ca2+-ATPases maintain steep calcium gradients\, internal
  Ca2+ stores\, and cytoplasmic free calcium at accurate levels that define
  and potentiate calcium signalling pathways. \nLipid flippases\, also of t
 he P-type ATPase family (P4-ATPases) maintain asymmetric lipid distributio
 ns in biomembranes. Their activity potentiates membrane dynamics\, but the
  structure and function of lipid flippases remained enigmatic until recent
 ly. We determined the first structures of lipid flippases using cryo-EM an
 d revealed at the same time a detailed insight into lipid recognition and 
 autoregulation.\nThe talk will cover methodological approaches supporting 
 the functional and mechanistic insight we have gained.\n\nhttps://lindico4
 53.srv.lu.se/event/125/contributions/752/
LOCATION:Kulturen Auditorium
URL:https://lindico453.srv.lu.se/event/125/contributions/752/
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