Cecropin
| Cecropin family | |||||||||
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| File:2IGR.pdb.png
2IGR ?
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| Identifiers | |||||||||
| Symbol | Cecropin | ||||||||
| Pfam | PF00272 | ||||||||
| InterPro | IPR000875 | ||||||||
| PROSITE | PDOC00241 | ||||||||
| SCOP | 1f0d | ||||||||
| SUPERFAMILY | 1f0d | ||||||||
| TCDB | 1.C.17 | ||||||||
| OPM superfamily | 160 | ||||||||
| OPM protein | 1d9j | ||||||||
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Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.
Cecropins[3][4][5] constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 31 - 37 amino acid residues active against both Gram-positive and Gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names; bactericidin, lepidopterin, sarcotoxin, etc. All of these peptides are structurally related.
Members
Members include :
- Cecropin A
- Peptide Sequence (KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK). Secondary structure includes two α helices.[6]:4.2 At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.[7]
- Cecropin B
- Peptide Sequence (KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL). Secondary structure includes two α helices.[6]:4.2
- CECD
- from Aedes aegypti (Yellowfever mosquito).[8]
- Papiliocin
- (A lepidopteran) from Papilio xuthus[8] an Asian swallowtail butterfly.
- Cecropin P1
- An antibacterial peptide from Ascaris suum, a parasitic nematode that resides in the pig intestine, also belongs to this family.
Derivatives
A derivative of Cecropin B is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.[9]
Some of the cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called anticancer peptides (ACPs).[6]:3 Hybrid ACPs based on Cecropin A have been studied for anticancer properties.[6]:7.1
References
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- Hoskin 2008 (above) section 4.2
External links
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- ↑ Cecropins at the US National Library of Medicine Medical Subject Headings (MeSH)
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ 6.0 6.1 6.2 6.3 Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567
- ↑ 8.0 8.1 cecropin family OPM
- ↑ Lua error in package.lua at line 80: module 'strict' not found. [<http://www.rcsb.org/pdb/explore/explore.do?structureId=2IGR> <Protein Data Bank>]
