Structural model of vinculin: Correlation of amino acid sequence with electron‐microscopical shape

FEBS Letters

Beck, Konrad¹ 

[1] Institute for Biophysics, Johannes Kepler University, Altenberger Strasse 69, A-4040 Linz-Auhof, Austria

关键词: Cytoskeleton;    Electron microscopy;    Protein structure;    Hydrodynamics;    Cell adhesion;   

DOI  :  10.1016/0014-5793(89)80002-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cytoskeleton-associated protein vinculin exhibits the shape of a ‘balloon on a string’ when examined by rotary shadowing electron microscopy. Recently, the complete primary structure of chicken vinculin was determined which leads to the questions as to whether the globule might be either hollow or disc shaped, or whether the electron micrographs resemble those of vinculin dimers. Based on a hydrodynamical theory, evidence is presented for the assumption that vinculin as a monomer consists of a compact spherical head 6 nm in diameter connected by a proline-rich domain to a rod-shaped tail about 20 nm in length.

【 授权许可】

Unknown