A molecular model for the tumour‐associated antigen, p97, suggests a Zn‐binding function
- 22 June 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 305 (1), 55-61
- https://doi.org/10.1016/0014-5793(92)80654-y
Abstract
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.Keywords
This publication has 33 references indexed in Scilit:
- HUMAN MELANOTRANSFERRIN (P97) HAS ONLY ONE FUNCTIONAL IRON-BINDING SITEFEBS Letters, 1992
- High-resolution X-ray studies on rabbit serum transferrin: preliminary structure analysis of the N-terminal half-molecule at 2.3 Å resolutionActa crystallographica Section B, Structural science, crystal engineering and materials, 1990
- Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolutionJournal of Molecular Biology, 1989
- A unique signature identifies a family of zinc‐dependent metallopeptidasesFEBS Letters, 1989
- Molecular structure of serum transferrin at 3.3-.ANG. resolutionBiochemistry, 1988
- Helix geometry in proteinsJournal of Molecular Biology, 1988
- TOM: a FRODO subpackage for protein-ligand fitting with interactive energy minimizationJournal of Molecular Graphics, 1987
- Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by x-ray crystallography: a novel class of transition-state analogs for zinc peptidasesBiochemistry, 1984
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Structure of thermolysin refined at 1.6 Å resolutionJournal of Molecular Biology, 1982