Solution structure of the monomeric variant of the chemokine MIP-1beta
Structural comparison of monomeric variants of the chemokine MIP-1beta having differing ability to bind the receptor CCR5.
CC chemokine MIP-1beta can function as a monomer and depends on Phe13 for receptor binding
High-resolution solution structure of the beta chemokine hMIP-1beta by multidimensional NMR
MIP-1beta, T-CELL ACTIVATION PROTEIN 2, ACT-2, LYMPHOCYTE ACTIVATION GENE-1 PROTEIN, LAG-1
1HUM is the dimeric MIP-1beta wild-type protein.
1VMP binds to CCR5 which is a natural receptor of MIP-1beta.
This structure was determined using standard 3D 15N or 13C edited NMR experiments.
The structure is based on a total 940 restraints, 851 distance constraints, 69 dihedral angle restraints, 20 distance restraints for 10 hydrogen bonds.
The initial fold was obtained by distance geometry and further refined by simulated annealing.
1-2mM MIP-1b F13A U-15N, 13C; 20mM Na-phosphate buffer
MIP-1beta, chemokine, macrophage inflammatory protein, ANTIVIRAL PROTEIN