4XX8: Crystal Structure Of Pro1 Deletion Mutant Of Human Macrophage Migration Inhibitory Factor

Citation:
Abstract
For more than 15 years, the tautomerase active site of macrophage migration inhibitory factor (MIF) and its catalytic residue Pro1 have been being targeted for the development of therapeutics that block activation of its cell surface receptor, CD74. Neither the biological role of the MIF catalytic site nor the mechanistic details of CD74 activation are well understood. The inherently unstable structure of CD74 remains the biggest obstacle in structural studies with MIF for understanding the basis of CD74 activation. Using a novel approach, we elucidate the mechanistic details that control activation of CD74 by MIF surface residues and identify structural parameters of inhibitors that reduce CD74 biological activation. We also find that N-terminal mutants located deep in the catalytic site affect surface residues immediately outside the catalytic site, which are responsible for reduction of CD74 activation.
PDB ID: 4XX8Download
MMDB ID: 133076
PDB Deposition Date: 2015/1/30
Updated in MMDB: 2015/10
Experimental Method:
x-ray diffraction
Resolution: 1.77  Å
Source Organism:
Similar Structures:
Biological Unit for 4XX8: trimeric; determined by author and by software (PISA)
Molecular Components in 4XX8
Label Count Molecule
Proteins (3 molecules)
3
Macrophage Migration Inhibitory Factor(Gene symbol: MIF)
Molecule annotation
Chemicals (8 molecules)
1
5
2
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.