Cecropin family | |||||||||
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![]() 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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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Cecropins are antimicrobial peptides. 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 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 include :
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.
Some of the cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called anticancer peptides (ACPs). Hybrid ACPs based on Cecropin A have been studied for anticancer properties.