Tubulin: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px|thumb|Crystal Structure of Tubulin [[1z5w]] {{STRUCTURE_1z5w| PDB=1z5w | SIZE=300| SCENE= |right|CAPTION=Tubulin 1z5w }} Tubulin (TUB) is a constit... |
Michal Harel (talk | contribs) No edit summary |
||
(43 intermediate revisions by 3 users not shown) | |||
Line 1: | Line 1: | ||
<StructureSection load='' size='350' side='right' caption='γ-tubulin complex with GTP and Mg+2 ion (green), [[1z5w]]' scene='43/430888/Cv/2' pspeed='8'> | |||
== Function == | |||
[[Tubulin]] (TUB) is a constituent of microtubules in eukaryotes. Microtubules are assembled from dimers of | [[Tubulin]] (TUB) is a constituent of microtubules in eukaryotes. Microtubules are assembled from dimers of '''α-tubulin''' (TUBA) and '''β-tubulin''' (TUBB) bound to GTP. '''γ-tubulin''' (TUBG) is part of the nucleation of microtubules<ref>PMID:11297925</ref>. Human TUB contains several numbered subtypes. Tubulin filaments are stabilized by taxol and zampanolide. '''FtsZ''' (Filamenting temperature-sensitive mutant Z) is a prokaryotic homologue of TUB<ref>PMID:26463348</ref>. See [[Cell division protein]] and [[Beta tubulin]]. | ||
== Relevance == | |||
The chemotherapeutic drug Taxol interacts with TUBB. See [[Molecular Playground/Taxol]]. TUBA and TUBB expression in polyps of invasive colon cancer is different from normal<ref>PMID:16101133</ref>. | |||
See [[Paclitaxel]]. | |||
== | == Disease == | ||
Mutations in TUBB underlie a large spectrum of neuronal migration disorders<ref>PMID:19465910</ref>. | |||
== Structural highlights == | |||
*<scene name='43/430888/Cv/6'>γ-tubulin interactions with GTP and Mg+2 ion</scene> ([[1z5w]]). | |||
== 3D Structures of Tubulin == | |||
[[Tubulin 3D Structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | |||