Skip NavigationSkip to Content
Return Return to Search Results

The structure of human macrophage inflammatory protein-3 alpha/CCL20 - Linking antimicrobial and CC chemokine receptor- 6-binding activities with human beta-defensins

  1. Author:
    Hoover, D. M.
    Boulegue, C.
    Yang, D.
    Oppenheim, J. J.
    Tucker, K.
    Lu, W. Y.
    Lubkowski, J.

  2. Author Address

    NCI, Macromol Crystallog Lab, POB B,Ft Detrick, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Mol Immunoregulat Lab, Frederick, MD 21702 USA NCI, Opportunist Infect Lab, Div Canc Treatment, Centers & Diag Dev Therapeut Program, Frederick, MD 21702 USA Univ Maryland, Inst Human Virol, Inst Biotechnol, Baltimore, MD 21201 USA Lubkowski J NCI, Macromol Crystallog Lab, POB B,Ft Detrick, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Journal of Biological Chemistry
    1. 277
    2. 40
    3. Pages: 37647-37654
  4. Type of Article: Article
  1. Abstract:

    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-3a 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-3a 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-3a refined to a resolution of 1.7 Angstrom 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.

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel