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Originally published In Press as doi:10.1074/jbc.M005085200 on November 1, 2000

J. Biol. Chem., Vol. 276, Issue 7, 4909-4916, February 16, 2001
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Solution Structure and Dynamics of Myeloid Progenitor Inhibitory Factor-1 (MPIF-1), A Novel Monomeric CC Chemokine*

Krishna RajarathnamDagger §, Yuling Li, Thomas Rohrer, and Reiner Gentz

From the Dagger  Department of Human Biological Chemistry and Genetics and Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555 and the  Department of Protein Expression, Human Genome Sciences, Inc., Rockville, Maryland 20850

MPIF-1, a CC chemokine, is a specific inhibitor of myeloid progenitor cells and is the most potent activator of monocytes. The solution structure of myeloid progenitor inhibitor factor-1 (MPIF-1) has been determined by NMR spectroscopy. The structure reveals that MPIF-1 is a monomer with a well defined core except for termini residues and adopts the chemokine fold of three beta -strands and an overlying alpha -helix. In addition to the four cysteines that characterize most chemokines, MPIF-1 has two additional cysteines that form a disulfide bond. The backbone dynamics indicate that the disulfide bonds and the adjacent residues that include the functionally important N-terminal and N-terminal loop residues show significant dynamics. MPIF-1 is a highly basic protein (pI >9), and the structure reveals distinct positively charged pockets that could be correlated to proteoglycan binding. MPIF-1 is processed from a longer proprotein at the N terminus and the latter is also functional though with reduced potency, and both proteins exist as monomers under a variety of solution conditions. MPIF-1 is therefore unique because longer proproteins of all other chemokines oligomerize in solution. The MPIF-1 structure should serve as a template for future functional studies that could lead to therapeutics for preventing chemotherapy-associated myelotoxicity.

* The purchase of NMR instruments was funded by the Government of Canada's Network of Centers of Excellence Program and the Medical Research Council of Canada. The ultracentrifuge core was supported by National Institutes of Health Grant RR08961.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1G91) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/). .

§ To whom correspondence should be addressed. Tel.: 409-772-2238; Fax: 409-772-1790; E-mail: krishna@hbcg.utmb.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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