2vr8

Crystal Structure of G85R ALS mutant of Human Cu,Zn Superoxide Dismutase (CuZnSOD) at 1.36 A resolutionCrystal Structure of G85R ALS mutant of Human Cu,Zn Superoxide Dismutase (CuZnSOD) at 1.36 A resolution

Structural highlights 2vr8 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , NonStd Res: , Related: 1l3n, 2af2, 1uxl, 1ptz, 1oez, 1rk7, 1hl4, 1azv, 2v0a, 2c9s, 4sod, 1mfm, 2vr6, 1ozu, 1dsw, 1ozt, 1kmg, 2c9v, 1n18, 1ba9, 1pu0, 1fun, 1sos, 1n19, 2c9u, 1hl5, 1p1v, 1uxm, 1spd, 2vr7 Activity: Superoxide dismutase, with EC number 1.15.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause a dominant form of the progressive neurodegenerative disease amyotrophic lateral sclerosis. Transgenic mice expressing the human G85R SOD1 variant develop paralytic symptoms concomitant with the appearance of SOD1-enriched proteinaceous inclusions in their neural tissues. The process(es) through which misfolding or aggregation of G85R SOD1 induces motor neuron toxicity is not understood. Here we present structures of the human G85R SOD1 variant determined by single crystal x-ray diffraction. Alterations in structure of the metal-binding loop elements relative to the wild type enzyme suggest a molecular basis for the metal ion deficiency of the G85R SOD1 protein observed in the central nervous system of transgenic mice and in purified recombinant G85R SOD1. These findings support the notion that metal-deficient and/or disulfide-reduced mutant SOD1 species contribute to toxicity in SOD1-linked amyotrophic lateral sclerosis. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.,Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ J Biol Chem. 2008 Jun 6;283(23):16169-77. Epub 2008 Mar 31. PMID:18378676 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Superoxide Dismutase

spinqualitylabelsall models 2vr8, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image