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- W2146385204 abstract "Haemocyanins are multimeric oxygen transport proteins, which bind oxygen to type 3 copper sites. Arthropod haemocyanins contain 75-kDa subunits, whereas molluscan haemocyanins contain 350–400-kDa subunits comprising seven or eight different 50 kDa FUs (functional units) designated FU-a to FU-h, each with an active site. FU-h possesses a tail of 100 amino acids not present in the other FUs. In the present study we show by X-ray crystallography that in FU-h of KLH1 (keyhole-limpet-haemocyanin isoform 1) the structure of the tail domain is cupredoxin-like but contains no copper. The copper-free domain 3 in arthropod haemocyanin subunits has also recently been reinterpreted as being cupredoxin-like. We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain." @default.
- W2146385204 created "2016-06-24" @default.
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- W2146385204 date "2010-02-24" @default.
- W2146385204 modified "2023-10-06" @default.
- W2146385204 title "Cupredoxin-like domains in haemocyanins" @default.
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- W2146385204 doi "https://doi.org/10.1042/bj20091501" @default.
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