Structural highlights
Function
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Publication Abstract from PubMed
Marine macrolide toxins of trisoxazole family target actin with high affinity and specificity and have promising pharmacological properties. We present X-ray structures of actin in complex with two members of this family, kabiramide C and jaspisamide A, at a resolution of 1.45 and 1.6 A, respectively. The structures reveal the absolute stereochemistry of these toxins and demonstrate that their trisoxazole ring interacts with actin subdomain 1 while the aliphatic side chain is inserted into the hydrophobic cavity between actin subdomains 1 and 3. The binding site is essentially the same as the one occupied by the actin-capping domain of the gelsolin superfamily of proteins. The structural evidence suggests that actin filament severing and capping by these toxins is also analogous to that of gelsolin. Consequently, these macrolides may be viewed as small molecule biomimetics of an entire class of actin-binding proteins.
Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin.,Klenchin VA, Allingham JS, King R, Tanaka J, Marriott G, Rayment I Nat Struct Biol. 2003 Dec;10(12):1058-63. Epub 2003 Oct 26. PMID:14578936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klenchin VA, Allingham JS, King R, Tanaka J, Marriott G, Rayment I. Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin. Nat Struct Biol. 2003 Dec;10(12):1058-63. Epub 2003 Oct 26. PMID:14578936 doi:10.1038/nsb1006
