1m8a
From Proteopedia
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|PDB= 1m8a |SIZE=350|CAPTION= <scene name='initialview01'>1m8a</scene>, resolution 1.70Å | |PDB= 1m8a |SIZE=350|CAPTION= <scene name='initialview01'>1m8a</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | + | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1ha6|1ha6]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8a OCA], [http://www.ebi.ac.uk/pdbsum/1m8a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m8a RCSB]</span> | ||
}} | }} | ||
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[[Category: Tucker, K.]] | [[Category: Tucker, K.]] | ||
[[Category: Yang, D.]] | [[Category: Yang, D.]] | ||
- | [[Category: IPA]] | ||
[[Category: cc-chemokine]] | [[Category: cc-chemokine]] | ||
[[Category: il-8 type dimer]] | [[Category: il-8 type dimer]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:41 2008'' |
Revision as of 19:12, 30 March 2008
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, resolution 1.70Å | |||||||
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Ligands: | |||||||
Related: | 1ha6
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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]. 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
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