Category Archives: Electron Cryo-microscopy
Scientists in Chris Tate’s group in the LMB’s Structural Studies Division have used electron cryo-microscopy to determine the structure of the serotonin receptor coupled to the heterotrimeric G protein Go, providing insights into how receptors bind specific G proteins.
Work from Harvey McMahon’s group in the LMB’s Neurobiology Division has uncovered how a protein, FCHSD2, controls actin polymerisation during endocytosis. Importantly the scientists discovered that FCHSD2 does its job from the area surrounding the site of endocytosis – making it the first description of an endocytic protein which localises to the flat region around endocytic events.
Genes are encoded in DNA and need to be copied into an intermediate mRNA molecule that contains the instructions to allow synthesis of protein. Almost every mRNA has a repetitive sequence at one end called a poly(A) tail. The length of this tail specifies the amount of time that the mRNA is present in the cell,
Alzheimer’s disease, the most common neurodegenerative disease, is characterised by the formation of filamentous Tau protein inside nerve cells and amyloid-beta peptides outside cells. Despite more than three decades of research into Tau filaments from a range of different neurodegenerative diseases,
Dyneins are a family of motor proteins that move along microtubules to transport various important cargos, including proteins and RNAs, to different parts of the cell and are crucial to correct cell function. Gradually, the structure of various components of dynein have been revealed.