Crystallization and Preliminary Crystallographic Studies of an Antitumour Lectin from the Edible Mushroom Agrocybe aegerita

Authors: Yang, Na; Liang, Yi; Xiang, Ye; Zhang, Ying; Sun, Hui; Wang, Da-Cheng

Source: Protein and Peptide Letters, Volume 12, Number 7, October 2005 , pp. 705-707(3)

Publisher: Bentham Science Publishers

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An antitumour lectin named AAL has been purified from the fruiting body of edible mushroom Agrocybe aegerita. In addition to having a distinct bioactivity, AAL shows strong inhibition effects on human and mouse tumour cells. It has been shown that AAL exerts its antitumour effects via apoptosis-induction. AAL and AAL-lactose complex have been crystallized and their diffraction data were collected with resolution of 2.6 Å and 3.0 Å, respectively. Both crystals belong to space group P 6122 with unit cell parameters a = 123.98 Å, b = 123.98 Å, c = 56.86 Å, a= b=90 , g = 120 and a = 123.69 Å, b = 123.69 Å, c = 56.64 Å, α= β=90 , γ = 120 , respectively.

Keywords: antitumour; apoptosis; crystallization; dnase activity; lectin; mushroom

Document Type: Review Article


Publication date: October 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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