Moricin
| Moricin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Solution structure of antibacterial peptide (Moricin) [1] | |||||||||
| Identifiers | |||||||||
| Symbol | Moricin | ||||||||
| Pfam | PF06451 | ||||||||
| InterPro | IPR009456 | ||||||||
| SCOP | 1kv4 | ||||||||
| SUPERFAMILY | 1kv4 | ||||||||
| OPM superfamily | 160 | ||||||||
| OPM protein | 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.[2][2] 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.[2][3] Moricin functions as an antibacterial peptide against Gram-positive and Gram-negative bacteria, with its main activity being towards Gram-positive bacteria.[2]
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 Lett. 518 (1-3): 33–8. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013.
- 1 2 3 4 5 "ScienceDirect - FEBS Letters : Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori".
- ↑ Hara S, Ishibashi J, Yamakawa M, Hemmi H (2002). "Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori". FEBS Lett. 518 (1-3): 33–38. doi:10.1016/S0014-5793(02)02637-6. PMID 11997013.
External links
This article incorporates text from the public domain Pfam and InterPro IPR009456
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