Sandbox Reserved 473: Difference between revisions

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== Structure ==

The structure of several kinesins have been elucidated primarily by X-ray crystallography, and also partly by electron microscopy <ref>Kull, F. J., Sablin, E.P., Lau, R., Fletterick, R.J., and Vale, R.D. (1996.) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature, 380: 550-55.</ref>. 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 <ref name = "goldstein">Goldstein, L.S.B. and Philp, A.V. (1999.) The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183.</ref>. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. 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. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind <ref name = "woehlke">Woehlke, G. and Schliwa, M. (2000.) Walking on two heads: the many talents of kinesin. Nature Rev. Mol. Cell Biol. 1, 50-58.</ref>.

The structure of several kinesins have been elucidated primarily by X-ray crystallography, and also partly by electron microscopy <ref>Kull, F. J., Sablin, E.P., Lau, R., Fletterick, R.J., and Vale, R.D. (1996.) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature, 380: 550-55.</ref>. The structure of conventional kinesin, a particular type of kinesin so named because it has been the most studied, is displayed in both the 2D and 3D figures shown. Conventional kinesin is a homodimer composed of two subunits, each with a heavy-chain (KHC) and light-chain (KLC) domain <ref name = "goldstein">Goldstein, L.S.B. and Philp, A.V. (1999.) The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183.</ref>. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. 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. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind <ref name = "woehlke">Woehlke, G. and Schliwa, M. (2000.) Walking on two heads: the many talents of kinesin. Nature Rev. Mol. Cell Biol. 1, 50-58.</ref>.

Key features within the motor domain include the <scene name='Sandbox_Reserved_473/Atp_binding_site/2'>ATP/ADP binding site</scene>, the <scene name='Sandbox_Reserved_473/Neck/1'>neck and neck linker</scene>, and the <scene name='Sandbox_Reserved_473/Relay_helix/1'>relay helix</scene>. 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 <ref name = "woehlke"/>.

Sandbox Reserved 473: Difference between revisions

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 == Structure ==
-The structure of several kinesins have been elucidated primarily by X-ray crystallography, and also partly by electron microscopy <ref>Kull, F. J., Sablin, E.P., Lau, R., Fletterick, R.J., and Vale, R.D. (1996.) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature, 380: 550-55.</ref>. 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 <ref name = "goldstein">Goldstein, L.S.B. and Philp, A.V. (1999.) The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183.</ref>. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. 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. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind <ref name = "woehlke">Woehlke, G. and Schliwa, M. (2000.) Walking on two heads: the many talents of kinesin. Nature Rev. Mol. Cell Biol. 1, 50-58.</ref>.
+The structure of several kinesins have been elucidated primarily by X-ray crystallography, and also partly by electron microscopy <ref>Kull, F. J., Sablin, E.P., Lau, R., Fletterick, R.J., and Vale, R.D. (1996.) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature, 380: 550-55.</ref>. The structure of conventional kinesin, a particular type of kinesin so named because it has been the most studied, is displayed in both the 2D and 3D figures shown. Conventional kinesin is a homodimer composed of two subunits, each with a heavy-chain (KHC) and light-chain (KLC) domain <ref name = "goldstein">Goldstein, L.S.B. and Philp, A.V. (1999.) The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183.</ref>. Together, these units form a protein composed of three main regions: the head, the stalk, and the tail. 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. The stalk and tail share little homology, suggesting the diversity of cargo that different kinesins bind <ref name = "woehlke">Woehlke, G. and Schliwa, M. (2000.) Walking on two heads: the many talents of kinesin. Nature Rev. Mol. Cell Biol. 1, 50-58.</ref>.
 Key features within the motor domain include the <scene name='Sandbox_Reserved_473/Atp_binding_site/2'>ATP/ADP binding site</scene>, the <scene name='Sandbox_Reserved_473/Neck/1'>neck and neck linker</scene>, and the <scene name='Sandbox_Reserved_473/Relay_helix/1'>relay helix</scene>. 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 <ref name = "woehlke"/>.