Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10767674 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
ARL5 is a member of ARLs, which is widespread in high eukaryotes and homologous between species. But no structure or biological function of this member is reported. We expressed, purified, and resolved the structure of human ARL5 with bound GDP3â²P at 2.0Â Ã
resolution. A comparison with the known structures of ARFs shows that besides the typical features of ARFs, human ARL5 has specific features of its own. Bacterially expressed human ARL5 contains bound GDP3â²P which is seldom seen in other structures. The hydrophobic tail of the introduced detergent Triton X-305 binds at the possible myristoylation site of Gly2, simulating the myristoylated state of N-terminal amphipathic helix in vivo. The structural features of the nucleotide binding motifs and the switch regions prove that ARL5 will undergo the typical GDP/GTP structural cycle as other members of ARLs, which is the basis of their biological functions.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Zhan-Xin Wang, Liang Shi, Jun-Feng Liu, Xiao-Min An, Wen-Rui Chang, Dong-Cai Liang,