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- W2023221864 abstract "The cytoskeleton-associated protein vinculin is composed of a globular head and an elongated tail domain. The protein can be cleaved by V8 protease treatment into two fragments with apparent molecular masses of 90 and 29/27 kDa, respectively. So far, no high-resolution data on the tertiary structure of the N-terminal 90-kDa fragment are available. We analyzed the 90-kDa fragment in detail, using electron spectroscopic imaging in conjunction with modelling experiments. The front view projection of this fragment appears roughly rhomboidal, with 4 intensity maxima arranged at the vertices and a stain-filled region in the center. Based on a detailed examination of different particle projections, a 3-dimensional model was constructed which appears as a flattened tetrahedron. A comparison of the 90-kDa fragment with the intact protein allows for a correlation between the subdomain organization of the vinculin head and the biochemically defined V8 protease cleavage sites (aa 851 and 857)." @default.
- W2023221864 created "2016-06-24" @default.
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- W2023221864 date "2001-03-01" @default.
- W2023221864 modified "2023-10-14" @default.
- W2023221864 title "3-Dimensional organization of the N-terminal vinculin head fragment" @default.
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- W2023221864 doi "https://doi.org/10.1078/0171-9335-00152" @default.
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