- 作者: Jack Cheng; Tian-Huey Lu; Chao-Lin Liu; Jung-Yaw Lin
- 作者服務機構: Department of Physics, National Tsing Hua University, Hsinchu, Taiwan, R.O.C.
- 中文摘要: --
- 英文摘要:
X-ray crystal structure determination of agglutinin from abrus precatorius in Taiwan is presented. The
crystal structure of agglutinin, a type II ribosome-inactivating protein (RIP) from the seeds of Abrus
precatorius in Taiwan, has been determined from a novel crystalline form by the molecular replacement
method using the coordinates of abrin-a as the template. The structure has space group P41212 with Z=8, and
been refined at 2.6Å to R-factor of 20.4%. The root-mean-square deviations of bond lengths and angles
from the standard values are 0.009Å and 1.3 º. Primary, secondary, tertiary and quaternary structures of
agglutinin have been described and compared with those of abrin-a to a certain extent. In subsequent
docking research, we found that Asn200 of abrin-a may form a critical hydrogen bond with G4323 of
28SRNA, while corresponding Pro199 of agglutinin is a kink hydrophobic residue bound with the cleft in a
more compact complementary relationship. This may explain the lower toxicity of agglutinin than abrin-a,
despite of similarity in secondary structure and the activity cleft of two RIPs. - 中文關鍵字: --
- 英文關鍵字: --