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http://purl.uniprot.org/citations/17070542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17070542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17070542http://www.w3.org/2000/01/rdf-schema#comment"The gain of neurotoxic function in amyotrophic lateral sclerosis (ALS) has been linked to misfolding of the homodimeric enzyme Cu/Zn superoxide dismutase (SOD). Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. A hallmark of this species is that it fails to dimerize and becomes trapped as a monomer in the absence of the active-site metals. The crystallographic data show that removal of the C57-C146 disulphide bond sets free the interface loop IV in the apo protein, whereas the same loop remains unaffected in the holo protein. Thus, the low dimerisation propensity of disulphide-reduced apoSOD seems to be of entropic origin due to increased loop flexibility in the monomeric state: in the disulphide-reduced holo protein this gain in configurational entropy upon splitting of the dimer interface is reduced by the metal coordination."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.09.048"xsd:string
http://purl.uniprot.org/citations/17070542http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.09.048"xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Logan D.T."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Logan D.T."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Oliveberg M."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Oliveberg M."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Hoernberg A."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Hoernberg A."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Marklund S.L."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/author"Marklund S.L."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/pages"333-342"xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/pages"333-342"xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/title"The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/title"The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase."xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/volume"365"xsd:string
http://purl.uniprot.org/citations/17070542http://purl.uniprot.org/core/volume"365"xsd:string
http://purl.uniprot.org/citations/17070542http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17070542
http://purl.uniprot.org/citations/17070542http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17070542