X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.

Structural highlights

2fxu is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric actin at a resolution of 1.35 A. The most notable aspect of the bistramide A-actin structure is an extensive hydrogen-bonding network established upon a deep penetration of the central segment of bistramide A into the actin-binding cleft between subdomains 1 and 3. The structure presents the first insight into the observed ability of bistramide A to modulate G-actin polymerization. The structural information combined with our ability to chemically modify the bistramide framework provides the basis for rational development of a series of new synthetic analogues as useful probes for studying actin cytoskeleton and as potential therapeutic leads.

Structure of bistramide A-actin complex at a 1.35 angstroms resolution.,Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA J Am Chem Soc. 2006 Mar 29;128(12):3882-3. PMID:16551075[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA. Structure of bistramide A-actin complex at a 1.35 angstroms resolution. J Am Chem Soc. 2006 Mar 29;128(12):3882-3. PMID:16551075 doi:10.1021/ja058319c

2fxu, resolution 1.35Å

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