Cupredoxin
IPR008972
Definition
Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free copper is toxic, even at very low concentrations, its homeostasis in living organisms is tightly controlled by subtle molecular mechanisms. In eukaryotes, before being transported inside the cell via the high-affinity copper transporters of the CTR family, the copper (II) ion is reduced to copper (I). In blue copper proteins such as Cupredoxin, the copper (I) ion form is stabilised by a constrained His2Cys coordination environment. This entry represents cupredoxin proteins, as well as structural homologues to cupredoxin. Structurally, the cupredoxin-like fold consists of a β-sandwich with 7 strands in 2 β-sheets, which is arranged in a Greek-key β-barrel PMID:11867755. Some of these proteins have lost the ability to bind copper. Proteins with a cupredoxin-type fold are found in the following family groups: Mono-domain cupredoxins, such as amicyanin, plastocyanin, pseudoazurin, plantacyanin, azurin, auracyanin, rusticyanin, stellacyanin, and mavicyanin. Multi-domain cupredoxins, such as nitrite reductase (2 domains of this fold), multicopper oxidase CueO, spore coat protein A, ascorbate oxidase (3 domains of this fold), laccase (3 domains of this fold), ceruloplamin (6 domains of this fold), and coagulation factor V. Red copper protein nitrocyanin and the C-terminal of nitrous oxide reductase. Quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II. Ephrin-a5 and ephrin-b2 ectodomain, which are related to cupredoxins but lack the metal-binding site. The N-terminal domain of protein arginine deiminase Pad1-4 and Pad6, related to cupredoxin but lack the metal-biding site.
20 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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