2v0a

File:2v0a.gif

spinqualitylabelsall models 2v0a, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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 [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. 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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