@article {Li:2001:0929-8665:81,
title = "Crystal Structure of Trichosanthes Kirilowii Lectin-1 and its Relation to the Type 2 Ribosome Inactivating Proteins",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2001",
volume = "8",
number = "2",
publication date ="2001-04-01T00:00:00",
pages = "81-87",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2001/00000008/00000002/art00001",
doi = "doi:10.2174/0929866013409625",
keyword = "momordica charantia, ribosome-inactivating proteins rips, trichosanthin, tri, trichisanthes kirilowii lectin, krl-1, bryonia dioica, bryodin, type 2 ribosome-inaactivating proteins rips, mmomorcharin",
author = "Li, M. and Chai, J. and Wang, Y.",
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.",
}