Abstract
Carboxy-truncated mutants of human MIF (MIF(1-104) and MIF(1-109)) were used in structure activity studies. CD spectroscopy revealed an overall structural similarity between the mutants and MIF. Denaturant-induced unfolding demonstrated that the C-terminus contributed significantly to the conformational stability of MIF. This appears to be due to the formation of two C-terminal β-strands. The mutants were enzymatically active, exhibiting half of the enzymatic redox activity of MIF. However, immunological analysis showed that deletion of both 5 and 10 C-terminal residues resulted in loss of the macrophage activating properties of MIF, providing functional evidence that the C-terminus is important for immunological activity and trimer formation. A more detailed study of the C-terminus may assist in identifying the molecular basis for the immunological and enzymatic activities of MIF.
Original language | English |
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Pages (from-to) | 226-232 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 414 |
Issue number | 2 |
DOIs | |
State | Published - 8 Sep 1997 |
Externally published | Yes |
Keywords
- Cytokine
- Macrophage migration inhibitor factor
- Mutagenesis
- Protein structure
- Structure activity study