کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1929921 | 1050477 | 2012 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Crystal structure of inactive form of Rab3B Crystal structure of inactive form of Rab3B](/preview/png/1929921.png)
Rab proteins are the largest family of ras-related GTPases in eukaryotic cells. They act as directional molecular switches at membrane trafficking, including vesicle budding, cargo sorting, transport, tethering, and fusion. Here, we generated and crystallized the Rab3B:GDP complex. The structure of the complex was solved to 1.9 Å resolution and the structural base comparison with other Rab3 members provides a structural basis for the GDP/GTP switch in controlling the activity of small GTPase. The comparison of charge distribution among the members of Rab3 also indicates their different roles in vesicular trafficking.
► This is the first structural information of human Rab3B.
► To provides a structural basis for the GDP/GTP switch in controlling the activity of Rab3.
► The charge distribution of Rab3B indicates its unique roles in vesicular trafficking.
Journal: Biochemical and Biophysical Research Communications - Volume 418, Issue 4, 24 February 2012, Pages 841–844