2vr7: Difference between revisions

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{{STRUCTURE_2vr7|  PDB=2vr7  |  SCENE=  }}  
{{STRUCTURE_2vr7|  PDB=2vr7  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION'''
===CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION===




==Overview==
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Mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause a dominant form of the progressive neurodegenerative disease amyotrophic lateral sclerosis (ALS). Transgenic mice expressing the human Gly85Arg (G85R) SOD1 variant develop paralytic symptoms concomitant with the appearance of SOD1-enriched proteinaceous inclusions in their neural tissues. The process(es) through which misfiolding or aggregation of G85R SOD1 induce motor neuron toxicity are 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 CNS 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 ALS.
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==About this Structure==
==About this Structure==
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[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zn superoxide dismutase]]
[[Category: Zn superoxide dismutase]]
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