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

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

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 2 , 2001

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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

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Article Details

Year: 2001
Page: [81 - 87]
Pages: 7
DOI: 10.2174/0929866013409625
Price: $58

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