Abstract
For the first time, the three-dimensional structure of a member of the copper-containing class of oxygen-carrying proteins—the haemocyanins—has been determined. The structure of Panulirus interruptus haemocyanin at 3.2 A resolution shows that each subunit of the 450,000-molecular weight hexamer is folded into three domains, and that the binuclear copper site is situated in the centre of the second domain. Amino acid sequence comparisons suggest that the polypeptide fold of P. interruptus haemocyanin is common to all arthropod haemocyanins.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
