PDBsum entry: 1g91

Cytokine

PDB id: 1g91

Contents

Protein chain

77 a.a. *

* Residue conservation analysis

PDB id:

1g91

Name:

Cytokine

Title:

Solution structure of myeloid progenitor inhibitory factor- 1 (mpif-1)

Structure:

Myeloid progenitor inhibitory factor-1. Chain: a. Synonym: mpif-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

K.Rajarathnam,Y.Li,T.Rohrer,R.Gentz

Key ref:

K.Rajarathnam et al. (2001). Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine. J Biol Chem, 276, 4909-4916. PubMed id: 11060285 DOI: 10.1074/jbc.M005085200

Date:

21-Nov-00 Release date: 07-Mar-01

Protein chain

P55773  (CCL23_HUMAN) -  C-C motif chemokine 23

Seq: 120 a.a.

Struc: 77 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: immune response (1 term)
• Biochemical function: chemokine activity (1 term)

DOI no: 10.1074/jbc.M005085200

J Biol Chem 276:4909-4916 (2001)

PubMed id: 11060285

Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine.

K.Rajarathnam, Y.Li, T.Rohrer, R.Gentz.

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.

Selected figure(s)

Figure 1.
Fig. 1. A, superposition of the 30 simulated annealing structures about the average structure. B, the same as in panel A except the N-terminal (1-10) and the C-terminal (67) residues have been omitted for clarity. C, a schematic representation of MPIF-1 in the same orientation as shown in panel B created using the program MOLMOL (52).

Figure 6.
Fig. 6. Surface charge distribution of MPIF-1 (A), MPIF-1 after rotating 180° (B), IL-8 (C), and MIP-1 (D) created using the program MOLMOL (52). The orientation is essentially the same as shown in Fig. 4. Positive and negatively charged regions are shown in blue and red, respectively.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 4909-4916) copyright 2001.

Figures were selected by an automated process.