Crystallization and Preliminary X-Ray Crystallographic Studies of Trichosanthin Delta C7

Authors: Li X.; Ding Y.; Too H.; Wang Z.; Liu Y.; Dong Y.; Shaw P.; Rao Z.

Source: Protein and Peptide Letters, Volume 9, Number 3, June 2002 , pp. 269-273(5)

Publisher: Bentham Science Publishers

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Abstract:

Trichosanthin (TCS) is a type I ribosome-inactivating protein (RIP) which possesses rRNA N-glycosidase activity. TCS has various pharmacological properties. It is possible to reduce the antigenicity of TCS by deleting up to seven C-terminal residues of TCS (TCS-C7) with minimal effect on its activity [1]. TCS-C7 has been crystallized and the crystal diffracted to 1.8 Å. It belongs to space group P21, with unit-cell parameters a=71.6Å, b=74.4Å, c=87.6Å, bgr =97.0°. It is given that there are four molecules per asymmetric unit.

Keywords: trichosan thin deltac7; rip; ribosome-inactivating protein; trichosanthin(tcs); tcs-c7

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408742

Publication date: 2002-06-01

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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.