Myosin steps backwards
Article Abstract:
It has been possible to identify a class VI myosin, which is believed to power movement of vesicles, that tracks towards the minus end of the actin filament. It was established that the class VI myosins have a large insertion at the transition from the motor core to the base of the alpha-helical lever, the converter domain. It is thought that this insertion permits the class VI myosin motors to move in the opposite direction from all other forms of myosin. Further research must establish whether the third class of linear motors, the dyneins, also have representatives that move in the opposite direction.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Fibres hinge on swapped domains
Article Abstract:
Two domains with some proteins adopt a structure attached by a loop, which can serve as a hinge due to which the protein might open up adopting a high-energy state. This result in formation of an open swapped dimer where the interface of the two domains is reformed which leads to a synergy between the runaway domain and the formation of an amyloid fibre backbone.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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