The amino acid sequence of actinoporin RTX-A (175 aa) from the sea anemone Radianthus macrodactylus was determined by sequencing of clones obtained via amplification of cDNA. It was established that RTX-A possessed high homology with HmgIII from Heteractis magnifica (87%) and StI, StII from Stichodactyla helianthus (84 and 87%, respectively). The analysis of structural and functional relationships within RTX-A was carried out. The some disagreement concerning to significant role of several amino acid residues for actinoporins exhibition of hemolytic activity was found.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The amino acid sequence of actinoporin RTX-A (175 aa) from the sea anemone Radianthus macrodactylus was determined by sequencing of clones obtained via amplification of cDNA. It was established that RTX-A possessed high homology with HmgIII from Heteractis magnifica (87%) and StI, StII from Stichodactyla helianthus (84 and 87%, respectively). The analysis of structural and functional relationships within RTX-A was carried out. The some disagreement concerning to significant role of several amino acid residues for actinoporins exhibition of hemolytic activity was found.
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| skos:exactMatch | |
| uniprot:name |
Toxicon
|
| uniprot:author |
Barsova E.,
Guzev K.,
Il'ina A.P.,
Issaeva M.,
Kozlovskaya E.,
Leychenko E.,
Lipkin A.,
Lukyanov S.,
Monastyrnaia M.M.
|
| uniprot:date |
2006
|
| uniprot:pages |
517-520
|
| uniprot:title |
Amino acid sequence of RTX-A's isoform actinoporin from the sea anemone, Radianthus macrodactylus.
|
| uniprot:volume |
47
|
| dc-term:identifier |
doi:10.1016/j.toxicon.2005.12.014
|