5xlz
From Proteopedia
The crystal structure of tubulin complexed with a benzylidene derivative of 9(10H)-anthracenone
Structural highlights
Function[TBA1B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [STMN4_RAT] Exhibits microtubule-destabilizing activity.[1] [2] [3] [TBB2B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). Publication Abstract from PubMedMicrotubules are composed of alphabeta-tubulin heterodimers and have been treated as highly attractive targets for antitumor drugs. A broad range of agents bind to tubulin and interfere with microtubule assembly, including colchicine binding site inhibitors (CBSIs). Tubulin Polymerization Inhibitor I (TPI1), a benzylidene derivative of 9(10H)-anthracenone, is a CBSI that inhibits the assembly of microtubules. However, for a long time, the design and development of anthracenone family drugs have been hindered by the lack of structural information of the tubulin-agent complex. Here we report a 2.3 A crystal structure of tubulin complexed with TPI1, the first structure of anthracenone family agents. This complex structure reveals the interactions between TPI1 and tubulin, and thus provides insights into the development of new anthracenone derivatives targeting the colchicine binding site. Structure of a benzylidene derivative of 9(10H)-anthracenone in complex with tubulin provides a rationale for drug design.,Cheng J, Wu Y, Wang Y, Wang C, Wang Y, Wu C, Zeng S, Yu Y, Chen Q Biochem Biophys Res Commun. 2017 Nov 2. pii: S0006-291X(17)32082-X. doi:, 10.1016/j.bbrc.2017.10.104. PMID:29102632[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Bos taurus | Chen, Q | Yu, Y | Cell cycle | Inhibitor | Tubulin
