Premium
Human melanotransferrin (p97) has only one functional iron‐binding site
Author(s) -
Baker Edward N.,
Baker Heather M.,
Smith Clyde A.,
Stebbins Mark R.,
Kahn Maria,
Hellström Karl Erik,
Hellström Ingegerd
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80060-t
Subject(s) - binding site , transferrin , chemistry , fluorescence , biochemistry , a site , peptide sequence , amino acid , iron binding proteins , stereochemistry , biophysics , biology , physics , quantum mechanics , gene
The iron‐binding properties of melanotransferrin, the tumour‐associated antigen also known as p97, have been investigated by UV/visible and fluorescence spectroscopy, amino acid sequence comparison, and modelling. These show that, in contrast to other transferrins, melanotransferrin binds only one Fe 3+ ion per molecule. The binding properties of its N‐terminal site are similar to other transferrins, but its C‐terminal site does not bind iron at all. The differences can be related to specific amino acid changes in the C‐terminal site.