Sandbox Reserved 1099: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
Dermcidin is a channel composed of 3 antiparallel dimers. | Dermcidin is a channel composed of 3 antiparallel dimers, and has a dimension of about 8x4 nm. | ||
* Monomer : | * Monomer : | ||
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The trimer is formed by salt bridges between 3 subunits. This bonds are managed again by the negatively and positively charged residues so hydrophilic residues. Polar amino acids can be localized in the bond area too. In total, 96 residues are ionizable and which are all facing toward the interior of the tunnel. However, the amino acids pointing toward the exterior are hydrophobic because they are able to interact with the acyl chain of the membrane. They play a role in the internalization in the membrane. | The trimer is formed by salt bridges between 3 subunits. This bonds are managed again by the negatively and positively charged residues so hydrophilic residues. Polar amino acids can be localized in the bond area too. In total, 96 residues are ionizable and which are all facing toward the interior of the tunnel. However, the amino acids pointing toward the exterior are hydrophobic because they are able to interact with the acyl chain of the membrane. They play a role in the internalization in the membrane. | ||
The bonds between monomers allow the formation of 6 lateral openings of a diameter of 1 nm. And the presence of small (such as polar amino acids) and positive residues may have an impact on the selection of ion entry. | The bonds between monomers allow the formation of 6 lateral openings of a diameter of 1 nm. And the presence of small (such as polar amino acids) and positive residues may have an impact on the selection of ion entry. | ||
*The zinc cofactors : | |||
The zinc ions are fundamental as if there are not here, the DCD is no longer a channel. And the high permeability and conductance of the channel is allowed by Zn2+. | |||
== Antimicrobial activity == | == Antimicrobial activity == | ||
