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1wua
From Proteopedia
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(New page: 200px<br /><applet load="1wua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wua, resolution 1.45Å" /> '''The structure of Apl...)
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Revision as of 03:33, 21 November 2007
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The structure of Aplyronine A-actin complex
Overview
Aplyronine A, isolated from the sea hare Aplysia kurodai, possesses an, exceedingly potent antitumor effect in vivo and it is one of the promising, candidates as an anticancer drug. This macrolide is known to depolymerize, F-actin and inhibit the polymerization of actin by forming a 1:1 complex, with monomeric actin. The first complex structure of actin-aplyronine A, was determined via a synchrotron X-ray analysis at a 1.45 A resolution. As, expected, aplyronine A binds to a hydrophobic cleft composed of subdomains, 1 and 3 of actin by intercalating its aliphatic tail part into the actin, molecule as do the other reported F-actin depolymerizing agents., Unexpectedly, this complex structure shows the specific structural, features around the trimethylserine moiety, revealed as an important, moiety of aplyronine A for cytotoxicity against HeLa cells. Combining this, result and our previous one, the moiety should strongly relate to the, specific biological activity of aplyronine A; i.e. a potent antitumor, effect.
About this Structure
1WUA is a Single protein structure of sequence from Oryctolagus cuniculus with CA, ATP and AP8 as ligands. Full crystallographic information is available from OCA.
Reference
Structure basis for antitumor effect of aplyronine a., Hirata K, Muraoka S, Suenaga K, Kuroda T, Kato K, Tanaka H, Yamamoto M, Takata M, Yamada K, Kigoshi H, J Mol Biol. 2006 Mar 3;356(4):945-54. Epub 2005 Dec 27. PMID:16406066
Page seeded by OCA on Wed Nov 21 05:40:40 2007
Categories: Oryctolagus cuniculus | Single protein | Hirata, K. | Kato, K. | Kigoshi, H. | Kuroda, T. | Muraoka, S. | Suenaga, K. | Takata, M. | Tanaka, H. | Yamada, K. | Yamamoto, M. | AP8 | ATP | CA | Aplyronine a | Macrolide | Marine sponge | Potent antitumor effect
