Sandbox Reserved 473: Difference between revisions
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{{Sandbox_Reserved_Robert_B_Rose_1}} | {{Sandbox_Reserved_Robert_B_Rose_1}} | ||
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Kinesin | |||
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== Introduction == | == Introduction == | ||
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The structure of several kinesins have been elucidated primarily by X-ray crystallography, but also by electron microscopy [7]. The structure of conventional kinesin, a particular type of kinesin so named because it has been the most studied, is displayed at right. Conventional kinesin is a homodimer composed of two subunits, each with a heavy-chain (KHC) and light-chain (KLC) domain [1][4]. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. (NEED A FIGURE) The tail is responsible for binding the cargo. The stalk usually consists of a structure similar to a coiled coil that helps to secure the two monomers together. The head, also known as the motor domain or the heavy chain, is responsible for microtubule binding and catalytic activity. This motor domain is the most conserved element among all kinesins, with 35% sequence homology across all kinesins [4]. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind [4]. | The structure of several kinesins have been elucidated primarily by X-ray crystallography, but also by electron microscopy [7]. The structure of conventional kinesin, a particular type of kinesin so named because it has been the most studied, is displayed at right. Conventional kinesin is a homodimer composed of two subunits, each with a heavy-chain (KHC) and light-chain (KLC) domain [1][4]. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. (NEED A FIGURE) The tail is responsible for binding the cargo. The stalk usually consists of a structure similar to a coiled coil that helps to secure the two monomers together. The head, also known as the motor domain or the heavy chain, is responsible for microtubule binding and catalytic activity. This motor domain is the most conserved element among all kinesins, with 35% sequence homology across all kinesins [4]. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind [4]. | ||
Key features within the motor domain include the ADP/ATP | Key features within the motor domain include the <scene name='Sandbox_Reserved_473/Atp_binding_site/1'>ADP/ATP binding site</scene>, the neck and neck linker, and the relay helix. The ATP-binding site consists of a P-loop motif common not only to kinesin, but also to myosin as well as several G-proteins which also have nucleotidase activity. This homology suggests a common ancestor among these proteins [4]. | ||
