NEUROSCI 223 Lecture Notes - Lecture 12: Point Mutation, Peroxisome, Homomeric
7 Apr 2016
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Document Summary
Temperature-sensitive mutation point mutation that affects folding of the protein, can still function at regular temperature. Regions that belong to the same folded module are shown in the same colour. The crystal structure of a dynamin dimer is shown below (minus the prds, which are thought to be unfolded), and is colour-coded to match the linear representation (created with pymol (schr dinger); protein data. | schematic representation of dynamin dimers and of helical dynamin polymers around a tubular template in two different orientations (with 90 rotation between them). The colour- coding of the domains matches the colours in part a (minus the prds, which are thought to project out of the polymerized helix). The approximate location of the bound nucleotide is highlighted in yellow (small circles). Dynamin polymerization occurs as a result of interactions between the "stalks" of dynamin monomers (interface 2) and between stalk dimers (interfaces 1 and 3). Cryo-electron microscopy image showing a helical polymer of purified.
