2MXQ
The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse
Summary for 2MXQ
| Entry DOI | 10.2210/pdb2mxq/pdb |
| NMR Information | BMRB: 25424 |
| Descriptor | Paneth cell-specific alpha-defensin 1 (1 entity in total) |
| Functional Keywords | antimicrobial protein |
| Biological source | Equus caballus (domestic horse,equine) |
| Total number of polymer chains | 1 |
| Total formula weight | 4086.81 |
| Authors | Jung, S.,Michalek, M.,Shomali, M.,Soennichsen, F.D. (deposition date: 2015-01-12, release date: 2015-04-22, Last modification date: 2024-11-20) |
| Primary citation | Michalek, M.,Jung, S.,Shomali, M.R.,Cauchard, S.,Sonnichsen, F.D.,Grotzinger, J. Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1. Biochem.Biophys.Res.Commun., 459:668-672, 2015 Cited by PubMed Abstract: Defensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. α-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric α-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids. PubMed: 25769951DOI: 10.1016/j.bbrc.2015.02.168 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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