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

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

Volume: 8 Issue: 2

Author(s): Ming Li, Ji Jie Chai, Yao Ping Wang, Ke Yi Wang and Ru Chang Bi

Affiliation:

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

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.

Cite this article as:

Li Ming, Chai Jie Ji, Wang Ping Yao, Wang Yi Ke and Bi Chang Ru, Crystal Structure of Trichosanthes Kirilowii Lectin-1 and its Relation to the Type 2 Ribosome Inactivating Proteins, Protein & Peptide Letters 2001; 8 (2) . https://dx.doi.org/10.2174/0929866013409625