Sandbox myosinkinesin

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Function

Kinesin is generally responsible for the transport of polypeptides and other large molecules throughout a single cell, such as moving the spindles during cell division. Kinesin can only move from the negative (-) end of microtubules to the positive (+) end. This means that kinesin only moves objects out towards the periphery of the cell and thus aids in the secretion of molecules or division of cells.

Disease

Kinesin are involved during mitosis, failure of kinesin to work properly can lead to trisomy and other meiosis/mitosis related diseases.

Structural highlights

This is the overall structure of a functional kinesin dimer.

Heavy Chain

It is the most conserved region amongst kinesin which consists of the head, neck, and tail. Usually contains eight core β-sheets and six major alpha helixes, most of these secondary structures are in different places in the primary sequence but line up in the tertiary structure.

Light Chain

Not technically part of the protein of kinesin or myosin itself, but its presence is necessary for activity. It regulates conformational changes within the protein.

Here is a picture of the light chains.

Head Head: Most conserved domain amongst all kinesin, it consists mainly of alpha helixes. Its tertiary structure usually includes a large cleft from the actin binding site to the ATP binding pocket. The head has the ability to bind microtubule on one site and bind ATP at another. This section undergoes the most conformational change and is responsible for the force that causes kinesin to move along the cytoskeleton. In kinesin, binding of ATP appears to have allosteric control over the binding of kinesin to the tubules, by a twisting of a β- sheet core, showing allosteric control between the subdomains within the protein.

Neck

Tail