2MXQ image
Deposition Date 2015-01-12
Release Date 2015-04-22
Last Version Date 2024-11-20
Entry Detail
PDB ID:
2MXQ
Title:
The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse
Biological Source:
Source Organism(s):
Equus caballus (Taxon ID: 9796)
Method Details:
Experimental Method:
Conformers Calculated:
100
Conformers Submitted:
10
Selection Criteria:
structures with the lowest energy
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Paneth cell-specific alpha-de
Gene (Uniprot):DEFA1
Chain IDs:A
Chain Length:34
Number of Molecules:1
Biological Source:Equus caballus
Ligand Molecules
Primary Citation
Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1.
Biochem.Biophys.Res.Commun. 459 668 672 (2015)
PMID: 25769951 DOI: 10.1016/j.bbrc.2015.02.168

Abstact

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.

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Primary Citation of related structures
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