A molecular model for the tumour‐associated antigen, p97, suggests a Zn‐binding function

FEBS Letters

Jhoti, Harren²  Garratt, Richard C.¹ 

[1] Instituto de Fisica y Quimica de Sào Carlos, Departamento de Fisica y Ciěncia dos Materials, Universidade de Sào Paulo, 13560 Sào Carlos SP, Brazil;Laboratory of Molecular Biophysics, Rex Richards Building, South Parks Road, Oxford, UK

关键词: Transferrin;    Zn-binding;    Molecular modelling;    Tumour antigen;    Metallopeptidase;    Thermolysin;   

DOI  :  10.1016/0014-5793(92)80654-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown