1m8a
From Proteopedia
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Human MIP-3alpha/CCL20
Overview
Human macrophage inflammatory protein-3alpha (MIP-3alpha; CCL20) is a, CC-type chemokine that binds to and activates CC chemokine receptor-6, (CCR6). Although MIP-3alpha does not share the binding site of CCR6 with, any other chemokine, human beta-defensin-1 and -2, small cationic, antimicrobial peptides, have also been found to bind to and activate CCR6., Conversely, we have found that MIP-3alpha possesses antibacterial activity, of greater potency than human beta-defensin-1 and -2 against Escherichia, coli ATCC 25922 and Staphylococcus aureus ATCC 29213, while having no, activity against the fungus Candida albicans. There is no clear sequence, similarity between beta-defensins and the chemokine MIP-3alpha, beyond an, abundance of cationic residues and the presence of disulfide bonds., Nonetheless, there are structural similarities between these three, proteins that allow their overlap of chemotactic and antimicrobial, activities. In this report, we describe the x-ray crystal structure of, human MIP-3alpha refined to a resolution of 1.7 A and compare it with the, crystal structures of human beta-defensin-1 and -2. Molecules of, MIP-3alpha and the beta-defensins seem to share few structural motifs that, are likely associated with their common biological activities.
About this Structure
1M8A is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of human macrophage inflammatory protein-3alpha /CCL20. Linking antimicrobial and CC chemokine receptor-6-binding activities with human beta-defensins., Hoover DM, Boulegue C, Yang D, Oppenheim JJ, Tucker K, Lu W, Lubkowski J, J Biol Chem. 2002 Oct 4;277(40):37647-54. Epub 2002 Jul 30. PMID:12149255
Page seeded by OCA on Fri Feb 15 16:22:40 2008
