Inroduction

Dear reader, welcome to my website!

The intention of this website is to provide an informal and accessible platform for fellow scientists to get in touch about research projects in structural molecular biology.

Throughout my career as a protein crystallographer in Russia, Sweden and the UK I have participated in X-ray crystallographic studies of proteins of various complexity including plant haemoglobin, staphyllococcal enterotoxin, calbindin mutants, fungal laccase, bacterial prismane, yeast fumarase, viral hemagglutinin-neuraminidase, bacterial aldolase and human ceruloplasmin.

I have selected a few these interesting ‘structure-function stories’ of proteins for this website. One of these is ceruloplasmin, which you will find in the menu above. This enzyme is a member of the evolutionary family of multicopper oxidases (MCO), which includes hephaestin, ascorbate oxidase, ferroxidase Fet3p, laccase and related to this family, blood coagulation factors V and VIII. Quite surprisingly, although not enzymes, factors V & VIII have evolutionary acquired the structure of ceruloplasmin for their triplicated A domains. Ceruloplasmin is also known as ‘an enigmatic copper protein’ due to its multifunctional (and often mysterious) physiological roles in the mammalian plasma blood. Together with my colleagues from Russia and the UK we have significantly contributed into the human ceruloplasmin (hCP) research project.

I am currently working on homology modelling and structural comparison of the MCO family proteins including the hCP mutant structures involved in aceruloplasminemia, an inherited genetic disorder which is caused by defects in the ceruloplasmin gene .

I hope you enjoy your reading! I will be happy to answer any questions or respond to suggestions for research you may have.

Kind regards, Dr Viatcheslav Zaitsev

e-mail: vz@st-andrews.ac.uk