Title : Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.

Pub. Date : 2013 Nov 29

PMID : 24427810






2 Functional Relationships(s)
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Protein Name
Organism
1 Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. Disulfides high mobility group box 1 Homo sapiens
2 The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA. Disulfides high mobility group box 1 Homo sapiens