4jd2 | pdb_00004jd2

Crystal structure of Bos taurus Arp2/3 complex binding with Mus musculus GMF

spinqualitylabelsall models 4jd2, resolution 3.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jd2 is a 8 chain structure with sequence from Bos taurus and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, CA, PG4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The Arp2/3 complex mediates formation of complex cellular structures such as lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is precisely controlled by over a dozen regulators, yet the structural mechanism by which regulators interact with the complex is unknown. GMF is a recently discovered regulator of the Arp2/3 complex that can inhibit nucleation and disassemble branches. We solved the structure of the 240-kDa assembly of Mus musculus GMF and Bos taurus Arp2/3 complex and found that GMF binds the barbed end of Arp2, overlapping with the proposed binding site of WASP-family proteins. The structure suggests that GMF can bind branch junctions in the manner that cofilin binds filament sides, consistent with a modified cofilin-like mechanism for debranching by GMF. The GMF-Arp2 interface reveals how the ADF-H actin-binding domain in GMF is exploited to specifically recognize Arp2/3 complex and not actin. Structural basis for regulation of Arp2/3 complex by GMF.,Luan Q, Nolen BJ Nat Struct Mol Biol. 2013 Jul 28. doi: 10.1038/nsmb.2628. PMID:23893131 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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