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Article

Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.

Proceedings of the National Academy of Sciences of the United States of America - 28 Apr 2009

Banci Lucia, Bertini Ivano, Boca Mirela, Calderone Vito, Cantini Francesca, Girotto Stefania, Vieru Miguela

Abstract excerpt

The structural and dynamical properties of the metal-free form of WT human superoxide dismutase 1 (SOD1) and its familial amyotrophic lateral sclerosis (fALS)-related mutants, T54R and I113T, were characterized both in solution, through NMR, and in the crystal, through X-ray diffraction. We found that all 3 X-ray structures show significant structural disorder in 2 loop regions that are, at variance, well defined...

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Topics

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Share to Apoproteins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Share to Superoxide Dismutase

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Source

Open in PubMed Open full text

Identifiers

PMID: 19369197
DOI: 10.1073/pnas.0809845106
PMCID: PMC2678485

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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