Crystal Structure of Trichosanthes Kirilowii Lectin-1 and its Relation to the Type 2 Ribosome Inactivating Proteins

Authors: Li M.; Chai J.Jie; Wang Y.Ping

Source: Protein and Peptide Letters, Volume 8, Number 2, April 2001 , pp. 81-87(7)

Publisher: Bentham Science Publishers

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Abstract:

Crystal structure of a two-chain lectin, isolated from the tuber of Trichosanthes kirilowii, was solved by the molecular replacement method using abrin-a as probe. From the present density map at 2.7A resolution, it could be seen that a residue corresponding to an invariant tyrosine locating in the active site of ribosome-inactivating proteins (RIPs) is replaced with a non-aromatic one. This may be the reason why this kind of lectins has no RIPs activity, even though they possess some properties similar to type 2 RIPs.

Keywords: trichisanthes kirilowii lectin; ribosome-inactivating proteins rips; type 2 ribosome-inaactivating proteins rips; tri; trichosanthin; momordica charantia; bryonia dioica; bryodin; mmomorcharin; krl-1

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409625

Publication date: 2001-04-01

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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.