From Wikipedia, the free encyclopedia
Moricin
Solution structure of antibacterial peptide (moricin) [1]
Identifiers
SymbolMoricin
Pfam PF06451
InterPro IPR009456
SCOP2 1kv4 / SCOPe / SUPFAM
OPM superfamily 151
OPM protein 1kv4
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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]

References

  1. ^ a b c d e 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.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR009456
From Wikipedia, the free encyclopedia
Moricin
Solution structure of antibacterial peptide (moricin) [1]
Identifiers
SymbolMoricin
Pfam PF06451
InterPro IPR009456
SCOP2 1kv4 / SCOPe / SUPFAM
OPM superfamily 151
OPM protein 1kv4
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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]

References

  1. ^ a b c d e 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.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR009456

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