title: Molecular-replacement studies of Trichosanthes kirilowii lectin 1: a structure belonging to the family of type 2 ribosome-inactivating proteins.
abstract: Trichosanthes kirilowii lectin 1 (TKL-1) isolated from the tuber of T. kirilowii consists of two chains, each with a molecular weight of about 30 kDa. It has immunological properties which are similar to some ribosome-inactivating proteins (RIPs). TKL-1 was crystallized in space group P2(1)2(1)2(1) and diffraction data were collected to 2.7 A resolution. The molecular-replacement method was applied to solve the structure, using different chains of ricin, abrin-a and trichosanthin as search models. A set of consistent solutions was further verified by R(omit) profile analysis. In addition, the spatial arrangement of the two chains of TKL-1 is identical to that of type 2 RIPs.
authors.affiliation: Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
authors.forename: M
authors.initials: M
authors.lastname: Li
authors.forename: Y P
authors.initials: YP
authors.lastname: Wang
authors.forename: J J
authors.initials: JJ
authors.lastname: Chai
authors.forename: K Y
authors.initials: KY
authors.lastname: Wang
authors.forename: R C
authors.initials: RC
authors.lastname: Bi
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D008970:Molecular Weight; D037121:Plant Lectins; D010946:Plants, Medicinal / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D012270:Ribosomes
chemical_list: D037102:Lectins; D037121:Plant Lectins