User:Alisa Cario

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== '''Function''' ==
== '''Function''' ==
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<scene name='77/778894/Stathmin/1'>Stathmin</scene>, also known as oncoprotein 18 or metablastin, is a 19kDa microtubule associated protein known to destabilize microtubules <ref>PMID:8598048</ref>. These proteins are cell cycle and developmentally regulated, known to play a role in proliferation, differentiation, and function of cells <ref>PMID:9312271</ref> <ref>PMID: 9880330</ref>. Stathmin family proteins can bind to <scene name='77/778894/Highlight_of_tubulin/1'>tubulin dimers</scene> to inhibit polymerization or can bind to the microtubule to enhance the rate of catastrophe<ref>PMID:8598048</ref>
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<scene name='77/778894/Stathmin/1'>Stathmin</scene>, also known as oncoprotein 18 or metablastin, is a 19kDa microtubule associated protein known to destabilize microtubules <ref>PMID:8598048</ref>. These proteins are cell cycle and developmentally regulated, known to play a role in proliferation, differentiation, and function of cells <ref>PMID:9312271</ref> <ref>PMID: 9880330</ref>. Stathmin family proteins can bind to <scene name='77/778894/Highlight_of_tubulin/1'>two tubulin dimers</scene> to inhibit polymerization or can bind to the microtubule to enhance the rate of catastrophe<ref>PMID:8598048</ref> The structure of stathmin-4, in 4eb6, is bound to two tubulin heterodimers. The tubulin dimers are bound to outside ligands. <scene name='77/778894/Vinblastine/1'>Vinblastine</scene> is a chemotherapeutic that binds to tubulin to prevent microtubule polymerization <ref>PMID: 1687171</ref>. The tubulin subunits are bound to <scene name='77/778894/Gtp_gdp_highlight_of_tubulin/1'>GTP/GDP.</scene> The beta subunits of tubulin are bound to GDP and each of the alpha subunits are bound to GTP and a Magnesium ion.
[[Image:Stathmin_figure_cario1.png|center|thumb| upright=3| Figure 1. Adapted from ''Ruben 2004''. Stathmin, in purple, can bind to tubulin dimers to prevent polymerization or to microtubules to increase the rate of catastrophe. ]]
[[Image:Stathmin_figure_cario1.png|center|thumb| upright=3| Figure 1. Adapted from ''Ruben 2004''. Stathmin, in purple, can bind to tubulin dimers to prevent polymerization or to microtubules to increase the rate of catastrophe. ]]
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[[Image:Stathmin_seq.png|center|thumb| upright=3| Figure 2. Stathmin structural domains related to amino acid sequence ]]
[[Image:Stathmin_seq.png|center|thumb| upright=3| Figure 2. Stathmin structural domains related to amino acid sequence ]]
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The structure of stathmin-4, in 4eb6, is bound to two tubulin heterodimers. The tubulin dimers are bound to outside ligands. <scene name='77/778894/Vinblastine/1'>Vinblastine</scene> is a chemotherapeutic that binds to tubulin to prevent microtubule polymerization <ref>PMID: 1687171</ref>. The tubulin subunits are bound to <scene name='77/778894/Gtp_gdp_highlight_of_tubulin/1'>GTP/GDP.</scene> The beta subunits of tubulin are bound to GDP and each of the alpha subunits are bound to GTP and a Magnesium ion. There are also <scene name='77/778894/Mutations_in_stathmin/1'>two mutations</scene> to stathmin-4 in this structure. The mutations at position 11 from an cysteine to an alanine and position 16 from a Phenylalanine to a Tryptophan.
 
====How does the structure relate to it's function?====
====How does the structure relate to it's function?====
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The<scene name='77/778894/Stathmin_c_term/1'> C-terminal region</scene>, also known as the interaction domain, is known to sequester tubulin heterodimers. This region is comprised of a <scene name='77/778894/Stathmin_coiled_coil/1'>coiled-coil alpha helix</scene>. This region of stathmin is <scene name='77/778894/Zoom_of_stathmin_on_alpha/1'>known to bind to helix 10 of alpha tubulin</scene>. Helix 10 of alpha tubulin is thought to be important for incorporation into microtubules <ref>PMID: 9880330</ref>. All members of this protein family contain the C-terminal coiled coil domain. However, the binding affinity to tubulin differs from protein family members <ref>PMID: 11278715</ref>
The<scene name='77/778894/Stathmin_c_term/1'> C-terminal region</scene>, also known as the interaction domain, is known to sequester tubulin heterodimers. This region is comprised of a <scene name='77/778894/Stathmin_coiled_coil/1'>coiled-coil alpha helix</scene>. This region of stathmin is <scene name='77/778894/Zoom_of_stathmin_on_alpha/1'>known to bind to helix 10 of alpha tubulin</scene>. Helix 10 of alpha tubulin is thought to be important for incorporation into microtubules <ref>PMID: 9880330</ref>. All members of this protein family contain the C-terminal coiled coil domain. However, the binding affinity to tubulin differs from protein family members <ref>PMID: 11278715</ref>
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There are <scene name='77/778894/Mutations_in_stathmin/1'>two mutations</scene> to stathmin-4 in this structure. The mutations at position 11 from an cysteine to an alanine and position 16 from a Phenylalanine to a Tryptophan.
== '''Disease relevance''' ==
== '''Disease relevance''' ==

Current revision

* Full Real Name: Alisa Cario

  • Position: Graduate Student
  • Institution (NO ABBREVIATIONS): University of Vermont
  • City, State/Province, Country: Burlington, VT USA
  • Field of Expertise or Study: Creation of protopedia page for a class project. The class is Proteins 1 under Dr. Stephen Everse


Stathmin-4 (RB3) bound to Tubulin stabilized with Vinblastine 

4eb6

PDB ID 4eb6

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Proteopedia Page Contributors and Editors (what is this?)

Alisa Cario, Eric Martz

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