4goy | pdb_00004goy

The crystal structure of human fascin 1 K41A mutant

spinqualitylabelsall models 4goy, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4goy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR, CL, DTT, GOL Related: 4gp0, 4gp3, 4gov Gene: FAN1, FSCN1, HSN, SNL (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Filopodia are cell surface protrusions that are essential for cell migration. This finger-like structure is supported by rigid tightly-bundled actin filaments. The protein responsible for actin-bundling in filopodia is fascin. However the mechanism by which fascin functions in filopodial formation is not clear. Here we provide biochemical, cryo-electron tomographic and X-ray crystal structural data demonstrating the unique structural characteristics of fascin. Systematic mutagenesis studies on 100 mutants of fascin indicate that there are two major actin-binding sites on fascin. Crystal structures of four fascin mutants reveal concerted conformational changes in fascin from inactive to active states in the process of actin bundling. Mutations in any one of the actin-binding sites impair the cellular function of fascin in filopodial formation. Altogether, our data reveal the molecular mechanism of fascin function in filopodial formation. Molecular Mechanism of Fascin Function in Filopodial Formation.,Yang S, Huang FK, Huang J, Chen S, Jakoncic J, Leo-Macias A, Diaz-Avalos R, Chen L, Zhang JJ, Huang XY J Biol Chem. 2012 Nov 26. PMID:23184945 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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