PDBsum entry: 1ha6

Immune system

PDB id: 1ha6

Contents

Protein chain

70 a.a. *

* Residue conservation analysis

PDB id:

1ha6

Name:

Immune system

Title:

Nmr solution structure of murine ccl20/mip-3a chemokine

Structure:

Macrophage inflammatory protein 3 alpha. Chain: a. Synonym: mip-3-alpha, cc chemokine larc

Source:

Synthetic: yes. Mus musculus. Mouse. Organism_taxid: 10090. Tissue: muscle. Cellular_location: secreted

NMR struc:

20 models

Authors:

J.M.Perez-Canadillas,A.Zaballos,J.Gutierrez,R.Varona, F.Roncal,J.P.Albar,G.Marquez,M.Bruix

Key ref:

J.M.Pérez-Cañadillas et al. (2001). NMR solution structure of murine CCL20/MIP-3alpha, a chemokine that specifically chemoattracts immature dendritic cells and lymphocytes through its highly specific interaction with the beta-chemokine receptor CCR6. J Biol Chem, 276, 28372-28379. PubMed id: 11373289 DOI: 10.1074/jbc.M103121200

Date:

28-Mar-01 Release date: 22-Aug-01

Protein chain

O89093  (CCL20_MOUSE) -  C-C motif chemokine 20

Seq: 97 a.a.

Struc: 70 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (2 terms)
• Biological process: immune response (3 terms)
• Biochemical function: protein binding (3 terms)

DOI no: 10.1074/jbc.M103121200

J Biol Chem 276:28372-28379 (2001)

PubMed id: 11373289

NMR solution structure of murine CCL20/MIP-3alpha, a chemokine that specifically chemoattracts immature dendritic cells and lymphocytes through its highly specific interaction with the beta-chemokine receptor CCR6.

J.M.Pérez-Cañadillas, A.Zaballos, J.Gutiérrez, R.Varona, F.Roncal, J.P.Albar, G.Márquez, M.Bruix.

ABSTRACT

CCL20/MIP-3alpha is a beta-chemokine expressed in the thymus, skin, and intestinal epithelial cells that exclusively binds and activates the CCR6 receptor in both mice and humans. The strict receptor binding specificity of CCL20 is exceptional; other chemokines and their receptors bind promiscuously with multiple partners. Toward determining the structural basis for the selective receptor specificity of CCL20, we have determined its three-dimensional structure by 1H NMR spectroscopy. CCL20 exhibits the same monomeric structure previously described for other chemokines: a three-stranded beta-sheet and an overlying alpha-helix. The CCL20 receptor selectivity could arise from the rigid conformation of the N-terminal DCCL motif as well as the groove between the N-loop and the beta2-beta3 hairpin, which is significantly narrower in CCL20 than in other chemokines. Similar structural features are seen in human beta-defensin 2, a small nonchemokine polypeptide reported to selectively bind and activate CCR6, which stresses their importance for the specific binding of both CCL20 and beta-defensin 2 to CCR6. CCL20's structure will be useful to design tools aimed to modulate its important biological functions.

Selected figure(s)

Figure 3.
Fig. 3. Stereoscopic views of the CCL20 solution structure. Superposition of the 20 structures with the N terminus on the right and the C terminus on the left side and -helix face (top) and N-loop face (middle). Bottom, ribbon representation of the lowest energy CCL20 structure in the N-loop face orientation.

Figure 6.
Fig. 6. Ribbon representation of the chemokine CCL20 (left) and the -defensin BD2 (37) (right). -Sheets are represented by arrows; arginine and lysine residues are shown in blue; Asp5 in CCL20 and Asp4 in BD2 are depicted in red; and Leu8 in CCL20 and Leu9 in BD2 are shown in green.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 28372-28379) copyright 2001.

Figures were selected by an automated process.