Moricin
Moricin is a highly basic antibacterial peptide that was isolated from the silkworm Bombyx mori.[1] It consists of a long alpha-helix with 8 turns from a 42 amino acid sequence over almost the entire protein.[1] 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.[1] Moricin functions as an antibacterial peptide against Gram-positive and Gram-negative bacteria, with its main activity being towards Gram-positive bacteria.[1]
| Moricin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Solution structure of antibacterial peptide (Moricin)[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Moricin | ||||||||
| Pfam | PF06451 | ||||||||
| InterPro | IPR009456 | ||||||||
| SCOP2 | 1kv4 / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 151 | ||||||||
| OPM protein | 1kv4 | ||||||||
| |||||||||
References
- Hemmi H, Ishibashi J, Hara S, Yamakawa M (May 2002). "Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori". FEBS Letters. 518 (1–3): 33–8. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013. S2CID 23886673.
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