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BEGIN:VEVENT
DTSTAMP:20260414T235147Z
DTSTART;VALUE=DATE-TIME:20250725T133000
DTEND;VALUE=DATE-TIME:20250725T143000
SUMMARY:Cellular Interfaces Seminar: Gap junctions at the membrane and th
 e space beneath? Professor Ramanathan Sowdhamini\, National Centre for B
 iological Sciences (TIFR)\, Bangalore
TZID:Europe/London
UID:20250725-8ac672c798095a1c0198095c5d7e003c@warwick.ac.uk
CREATED:20250724T102621Z
DESCRIPTION:Abstract: Protein-protein interactions are crucial for carryi
 ng out biological functions and for regulating activities. I will be pre
 senting two stories in this direction: membrane-bound channels and the a
 ctin-tropomyosin matrix proteins. Gap junction proteins orchestrate acro
 ss cells to form channels that permit cytosolic molecules such as glutam
 ate and ATP to leak into the extracellular medium. Innexins in worms and
  connexins in eukaryotes belong to this superfamily to perform these fun
 ctions. Interestingly\, despite their functional similarities\, their ol
 igomeric states are different. Innexins form octamers\, while connexins 
 for hexamers. Pannexins are intermediate sequences which form only hepta
 meric hemichannels\, but not functional channels. We asked a general que
 stion about the oligomeric preferences of the superfamily members by sim
 ply threading the alternate quaternary states and compared the interface
  psuedoenergies through an in-house algorithm called PPCheck (Sukhwal an
 d Sowdhamini\, 2015). There are various isomers of these proteins and we
  also examined few combinations of oligomers through modelling approache
 s. Results indicate that considerable specificity is achieved through N-
 terminal loop regions and hemi-channel interfaces. Actin-tropomyosin int
 eractions are crucial for biological processes such as muscle contractio
 n including cardiac muscles. Whereas the coiled-coil of human tropomyosi
 n\, TPM1\, interacts with seven molecules of actin\, all along its perio
 ds of heptad repeats\, we examined shorter length tropomyosins (such as 
 TPM4 and yeast homologue which binds to only four actins) through succes
 sive docking and energy calculations to compare the actin-tropomyosin in
 terface. I will discuss the results which indicate shorter length tropom
 yosins bind more strongly at the heptads. These might be compensatory me
 chanisms to combat the length differences. It will be interesting to fol
 low on biophysical validations and the functional basis of length variat
 ions amongst homologous proteins.
LOCATION:A151\, Medical School Building
CATEGORIES:BiomedicalSciences,Cellular Interfaces Seminar
LAST-MODIFIED:20250724T102621Z
ORGANIZER;CN=Jas Bains:
END:VEVENT
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