1uxm

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spinqualitylabelsall models 1uxm, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

A4V MUTANT OF HUMAN SOD1

Overview

More than 90 point mutations in human CuZn superoxide dismutase lead to, the development of familial amyotrophic lateral sclerosis, known also as, motor neuron disease. A growing body of evidence suggests that a subset of, mutations located close to the dimeric interface can lead to a major, destabilization of the mutant enzymes. We have determined the crystal, structures of the Ala4Val (A4V) and Ile113Thr (I113T) mutants to 1.9 and, 1.6 A, respectively. In the A4V structure, small changes at the dimer, interface result in a substantial reorientation of the two monomers. This, effect is also seen in the case of the I113T crystal structure, but to a, smaller extent. X-ray solution scattering data show that in the solution, state, both of the mutants undergo a more pronounced conformational ... [(full description)]

About this Structure

1UXM is a [Single protein] structure of sequence from [Homo sapiens] with CU and ZN 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

Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants., Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Doucette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5976-81. Epub 2004 Mar 31. PMID:15056757

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