1G91
SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)
Summary for 1G91
| Entry DOI | 10.2210/pdb1g91/pdb |
| Descriptor | MYELOID PROGENITOR INHIBITORY FACTOR-1 (1 entity in total) |
| Functional Keywords | chemokine, cytokine, mpif-1, ckb8, ccl23 |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8869.38 |
| Authors | Rajarathnam, K.,Li, Y.,Rohrer, T.,Gentz, R. (deposition date: 2000-11-21, release date: 2001-03-07, Last modification date: 2024-11-06) |
| Primary citation | Rajarathnam, K.,Li, Y.,Rohrer, T.,Gentz, R. Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine. J.Biol.Chem., 276:4909-4916, 2001 Cited by PubMed Abstract: 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. PubMed: 11060285DOI: 10.1074/jbc.M005085200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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