Antimicrobial dermcidin, DCD. Based on 3-d structural data, dermcidin forms an architecture of high-conductance transmembrane channels,
composed of zinc-connected trimers of antiparallel helix pairs.
Molecular dynamics simulations elucidated the unusual membrane permeation
pathway for ions and showed adjustment of the pore to various membranes (Song et al. 2013). DCD assembles in solution into a hexameric pre-channel complex before targeting the membrane and integration, the complex follows a deviation of the barrel stave model (Zeth and Sancho-Vaello 2017). The tilt angle and the conductance is determined by the membrane thickness and the cholesterol composition (Song et al. 2019). A soluble 48 residue fragment has been structurally characterized (PDB: 2KSG_A). Membrane interactions and pore formation have been investigated for α-helical
AMPs leading to the formulation of three basic mechanistic models: the
barrel stave, toroidal, and carpet models. Human
cathelicidin (LL-37) and dermcidin (DCD) are α-helical, and their structures have been solved at atomic
resolution. DCD assembles in solution into a hexameric pre-channel
complex before actual membrane targeting and integration steps
occur, and the complex follows a deviation of the barrel stave model (Zeth and Sancho-Vaello 2017).
|Species:||Homo sapiens (Human)  |
|Number of TMSs:||1|
|Location1 / Topology2 / Orientation3:
1: MRFMTLLFLT ALAGALVCAY DPEAASAPGS GNPCHEASAA QKENAGEDPG LARQAPKPRK
61: QRSSLLEKGL DGAKKAVGGL GKLGKDAVED LESVGKGAVH DVKDVLDSVL