کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767674 | 1050795 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
2.0Â Ã
crystal structure of human ARL5-GDP3â²P, a novel member of the small GTP-binding proteins
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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![عکس صفحه اول مقاله: 2.0Â Ã
crystal structure of human ARL5-GDP3â²P, a novel member of the small GTP-binding proteins 2.0Â Ã
crystal structure of human ARL5-GDP3â²P, a novel member of the small GTP-binding proteins](/preview/png/10767674.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 332, Issue 3, 8 July 2005, Pages 640-645
Journal: Biochemical and Biophysical Research Communications - Volume 332, Issue 3, 8 July 2005, Pages 640-645
نویسندگان
Zhan-Xin Wang, Liang Shi, Jun-Feng Liu, Xiao-Min An, Wen-Rui Chang, Dong-Cai Liang,