2wko | pdb_00002wko

STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.

spinqualitylabelsall models 2wko, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wko 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: CU, IOD, ZN NonStd Res: ACE, CSO Related: 1l3n, 2af2, 1uxl, 1ptz, 1oez, 2vr8, 1rk7, 2vr7, 1hl4, 1azv, 2c9s, 1mfm, 2v0a, 4sod, 1ozu, 1dsw, 2vr6, 1kmg, 1ozt, 2c9v, 1n18, 1ba9, 1pu0, 1fun, 1sos, 1n19, 2c9u, 1hl5, 1p1v, 1spd, 1uxm, 3gzo, 3gzp, 3gzq Activity: Superoxide dismutase, with EC number 1.15.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Amyotrophic lateral sclerosis (ALS) is a fatal, progressive neurodegenerative disease characterized by the destruction of motor neurons in the spinal cord and brain. A subset of ALS cases are linked to dominant mutations in copper-zinc superoxide dismutase (SOD1). The pathogenic SOD1 variants A4V and G93A have been the foci of multiple studies aimed at understanding the molecular basis for SOD1-linked ALS. The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease. Here we report the three-dimensional structures of metal-free A4V and of metal-bound and metal-free G93A SOD1. In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1 proteins. Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.,Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ Arch Biochem Biophys. 2009 Dec;492(1-2):40-7. Epub 2009 Oct 1. PMID:19800308 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Superoxide Dismutase

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