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: 10.2174/0929866013409625

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