Moricin

Moricin
Moricin
1KV4.pdb.jpg
Solution structure of antibacterial peptide (Moricin) [1]
Identifiers
Symbol Moricin
Pfam PF06451
InterPro IPR009456
SCOP 1kv4

Moricin is a highly basic antibacterial peptide that was isolated from the silkworm Bombyx mori. [2] It consists of a long alpha-helix with 8 turns from a 42 amino acid sequence over almost the entire protein. The entire protein is 71% helical, with exception to 4 N terminal residues and 6 C terminal residues.[2] With this data, we can conclude that the majority of the protein consists of alpha helix.[3] These alpha helices are considered coiled coils. [2] The N terminus of the helix is amphipathic, and the C terminus of the helix is predominately hydrophobic. The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria.[4] With this being said, this segment of the alpha helix is the active center of moricin for antibacterial activity. [2] Moricin functions as an antibacterial against gram positive and gram negative bacteria, with its main activity being towards gram positive bacteria.[2] However, the exact role of moricin in our immune system is unknown.

References

External links

This article includes text from the public domain Pfam and InterPro IPR009456


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