کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5505728 | 1400276 | 2017 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structure-activity relationships of Ï-Agatoxin IVA in lipid membranes
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
To analyze structural features of Ï-Aga IVA, a gating modifier toxin from spider venom, we here investigated the NMR solution structure of Ï-Aga IVA within DPC micelles. Under those conditions, the Cys-rich central region of Ï-Aga IVA still retains the inhibitor Cys knot motif with three short antiparallel β-strands seen in water. However, 15N HSQC spectra of Ï-Aga IVA within micelles revealed that there are radical changes to the toxin's C-terminal tail and several loops upon binding to micelles. The C-terminal tail of Ï-Aga IVA appears to assume a β-turn like conformation within micelles, though it is disordered in water. Whole-cell patch clamp studies with several Ï-Aga IVA analogs indicate that both the hydrophobic C-terminal tail and an Arg patch in the core region of Ï-Aga IVA are critical for Cav2.1 blockade. These results suggest that the membrane environment stabilizes the structure of the toxin, enabling it to act in a manner similar to other gating modifier toxins, though its mode of interaction with the membrane and the channel is unique.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 1, 1 January 2017, Pages 170-175
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 1, 1 January 2017, Pages 170-175
نویسندگان
Jae Ha Ryu, Hoi Jong Jung, Shiro Konishi, Ha Hyung Kim, Zee-Yong Park, Jae Il Kim,