1g91

From Proteopedia

Revision as of 13:51, 15 February 2008

SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)

Overview

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.

About this Structure

1G91 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine., Rajarathnam K, Li Y, Rohrer T, Gentz R, J Biol Chem. 2001 Feb 16;276(7):4909-16. Epub 2000 Nov 1. PMID:11060285

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