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A molecular model for the tumour‐associated antigen, p97, suggests a Zn‐binding function
Author(s) -
Garratt Richard C.,
Jhoti Harren
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)80654-y
Subject(s) - function (biology) , antigen , chemistry , biophysics , microbiology and biotechnology , computational biology , biochemistry , biology , immunology
The primary structure of p97 (melanotransferrin) has been compared with other members of the transferrin superfamily. A molecular structure of p97 has been modelled based on the crystal structure of diferric rabbit serum transferrin. The most significant amino acid substitutions in p97 are almost exclusively limited to only two regions; the C‐lobe iron‐binding cleft and the interlobe contact region. The latter includes within the N‐terminal lobe a Zn‐binding consensus sequence found in metallopeptidases, and in the C‐terminal lobe a glutamic acid residue (Glu‐394) capable of completing a potential thermolysin‐like Zn‐binding site. Thus, p97 may have a Zn‐binding potential, unique amongst the transferrin superfamily.