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Revision as of 18:37, 29 October 2007

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spinqualitylabelsall models 2v0a, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE

Overview

Mutations of the gene encoding Cu-Zn superoxide dismutase (SOD1) cause 20%, of the familial cases of the progressive neurodegenerative disease ALS. A, growing body of evidence suggests that in familial ALS (FALS) it is the, molecular behavior of the metal-depleted SOD1 dimer that leads to a gain, of toxic properties by misfolding, unfolding, and aggregation. Structural, studies have so far provided static snapshots on the behavior of the, wild-type enzyme and some of the FALS mutants. New approaches are required, to map out the structural trajectories of the molecule. Here, using our, 1.15-A resolution structure of fully metallated human SOD1 and highly, parallelized molecular dynamics code on a high-performance capability, computer, we have undertaken molecular dynamics calculations to ... [(full description)]

About this Structure

2V0A is a [Single protein] structure of sequence from [Homo sapiens] with CU, ZN, SO4 and ACT as [ligands]. Active as [[1]], with EC number [1.15.1.1]. Full crystallographic information is available from [OCA].

Reference

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase., Strange RW, Yong CW, Smith W, Hasnain SS, Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10040-4. Epub 2007 Jun 4. PMID:17548825

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