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TitleDimer Destabilization in Superoxide Dismutase May Result in Disease-Causing Properties: Structures of Motor Neuron Disease Mutants
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 101, Page 5976-, Year 2004
Publish dateFeb 25, 2004 (structure data deposition date)
AuthorsHough, M.A. / Grossmann, J.G. / Antonyuk, S.V. / Strange, R.W. / Doucette, P.A. / Rodriguez, J.A. / Whitson, L.J. / Hart, P.J. / Hayward, L.J. / Valentine, J.S. / Hasnain, S.S.
External linksProc. Natl. Acad. Sci. USA / PubMed:15056757
MethodsX-ray diffraction
Resolution1.6 - 1.9 Å
Structure data

PDB-1uxl:
I113T mutant of human SOD1
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-1uxm:
A4V mutant of human SOD1
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / HUMAN CU / ZN SUPEROXIDE DISMUTASE / ANTIOXIDANT / METAL- BINDING / AMYOTROPHIC LATERAL SCLEROSIS / DISEASE MUTATION

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