1G91
SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)
1G91 の概要
| エントリーDOI | 10.2210/pdb1g91/pdb |
| 分子名称 | MYELOID PROGENITOR INHIBITORY FACTOR-1 (1 entity in total) |
| 機能のキーワード | chemokine, cytokine, mpif-1, ckb8, ccl23 |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 8869.38 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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