http://purl.uniprot.org/citations/17070542 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17070542 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17070542 | http://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/17070542 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2006.09.048"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2006.09.048"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Logan D.T."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Logan D.T."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Oliveberg M."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Oliveberg M."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Hoernberg A."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Hoernberg A."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Marklund S.L."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/author | "Marklund S.L."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/pages | "333-342"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/pages | "333-342"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://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/17070542 | http://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/17070542 | http://purl.uniprot.org/core/volume | "365"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://purl.uniprot.org/core/volume | "365"xsd:string |
http://purl.uniprot.org/citations/17070542 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17070542 |
http://purl.uniprot.org/citations/17070542 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17070542 |