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CCS (gene)
Copper chaperone for superoxide dismutase is a metalloprotein that is responsible for the delivery of Cu to superoxide dismutase (SOD1). CCS is a 54kDa protein that present in mammals and most eukaryotes including yeast. The structure of CCS is composed of three distinct domains that are necessary for its function. Although CCS is important for many organisms, there are CCS independent pathways for SOD1, and many species lack CCS all together, such as ''C. elegans''.〔 In humans the protein is encoded by the ''CCS'' gene.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9973 )〕
== Structure and function ==
CCS is composed of three domains.〔 Domain I is located on the N-terminus and contains the MXCXXC Cu binding sequence.〔 It has been determined to be necessary for function of CSS but its specific role is currently unknown.〔 The structure of domain II greatly resembles that of SOD1 which allows it to perform the function of binding to SOD1.〔 Domain III contains a CXC Cu binding motif and performs the Cu insertion and subsequent disulfide oxidation of SOD1.〔
When CCS docks to SOD1, cysteine 244 of CCS and 57 of SOD1 form a disulfide linkage.〔 This disulfide bond is then transferred to form a disulfide bridge between cysteine 57 and 146 of SOD1.〔 CCS's catalytic oxidation of SOD1's disulfide bridge can only be performed in the presence of oxygen.〔 Furthermore, the disulfide linkage of SOD1 can be performed without the presence of CCS but requires oxygen and is much slower.〔 Additionally, CCS is proposed to help the proper folding of SOD1 by binding in the apo-state.〔
As well as SOD1, ''CCS'' (gene) has been shown to interact with APBA1.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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