Sandbox Reserved 1099
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | Dermcidin has a form of a channel composed of | + | Dermcidin has a form of a channel composed of 3 antiparallel dimers. |
* Monomer : | * Monomer : | ||
A monomer is formed by 2 elongated α-helix tied with 2 zinc ions. These Zn2+ ions are linked by N and C-terminal residues from each α-helix. The residues involved are charged amino acids such as E, D and H. | A monomer is formed by 2 elongated α-helix tied with 2 zinc ions. These Zn2+ ions are linked by N and C-terminal residues from each α-helix. The residues involved are charged amino acids such as E, D and H. | ||
| - | displays two interfaces to the other subunits. The first one interface, the extended one, is mainly composed of salt bridges. | ||
* Assembly of three monomers : | * Assembly of three monomers : | ||
| - | + | The trimer is formed by salt bridges between 3 subunits. This bonds are managed again by the negatively and positively charged residues. In total, 96 residues are ionizabled which are oriented toward the interior of the tunnel. But including 12 negative charges in total. Thus, there are a total of six Zn2+ ions so 2 per subunit. | |
| - | 96 residues are ionizabled which are oriented toward the interior of the tunnel. But including 12 negative charges in total. Thus, there are a total of six Zn2+ ions so 2 per subunit. | + | |
size, proteolytically processed, helix-hinge-helix | size, proteolytically processed, helix-hinge-helix | ||
Revision as of 08:53, 12 January 2020
| This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115. |
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Dermcidin is a Human antimicrobial peptide of 110 amino acids presents in sweat involved in the regulation of skin flora. This molecule encoded by the DCD gene plays a role in the host defense system as a trimeric channel and thus, is able to prevent infection after injuries or any skin disorders.
Contents |
Expression and function
Dermcidin gene is located on the chromosome 12 and expressed as precursor only in mucous cells of eccrine sweat glands within the dermis of the skin and the derived-peptide is then secreted by granules in sweat.
The molecular weight of the DCD full-length sequence is 9,3 kDa including the signal peptide.
The active form also named DCD-1L contains the C-terminal end from the 63 to the 110 residue and is probably created by combination of proteases in sweat under specific conditions. Indeed, the clivage could happen because the sweat is acidic and composed of salt concentration such as sodium, chloride, potassium and magnesium. This form is involved in the innate immune system and protect from a variety of pathogenic microorganisms.
The Dermcidin peptide sequence has no homology with other known antimicrobial peptides. Two classes of mammalian antimicrobial peptides exist :
- Cathelicidins
- Defensins which are cationic peptides (α-defensins and β-defensins)
But, some size and structural similarities can be found with the defensin family.
Structural highlights
Dermcidin has a form of a channel composed of 3 antiparallel dimers.
- Monomer :
A monomer is formed by 2 elongated α-helix tied with 2 zinc ions. These Zn2+ ions are linked by N and C-terminal residues from each α-helix. The residues involved are charged amino acids such as E, D and H.
- Assembly of three monomers :
The trimer is formed by salt bridges between 3 subunits. This bonds are managed again by the negatively and positively charged residues. In total, 96 residues are ionizabled which are oriented toward the interior of the tunnel. But including 12 negative charges in total. Thus, there are a total of six Zn2+ ions so 2 per subunit.
size, proteolytically processed, helix-hinge-helix
|
Antimicrobial activity
Related disease
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