| Literature DB >> 10614824 |
E A Pastorello1, C Ortolani, C Baroglio, V Pravettoni, M Ispano, M G Giuffrida, D Fortunato, L Farioli, M Monza, L Napolitano, M Sacco, E Scibola, A Conti.
Abstract
The major protein allergen of peach (Prunus persica), Pru p 1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p 1, obtained by direct amino acid sequence and liquid chromatography-mass spectrometry (LC-MS) analyses with the purified protein, is described here. The protein consists of 91 amino acids with a calculated molecular mass of 9178 Da. The amino acid sequence contains eight strictly conserved cysteines, as do all known LTPs, but secondary structure predictions failed to classify the peach 9 kDa protein as an 'all-alpha type', due to the high frequency of amino acids (nine prolines) disrupting alpha helices. Although the sequence similarity with maize LTP is only 63%, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP 16 are identical and 7 similar in the peach homolog, supporting the hypothesis of a similar function.Entities:
Mesh:
Substances:
Year: 1999 PMID: 10614824 DOI: 10.1515/BC.1999.167
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915