کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882062 | 1536535 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mechanism of interaction of PITPα with membranes: Conformational changes in the C-terminus associated with membrane binding
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Eukaryotic phosphatidylinositol transfer proteins (PITPs) are composed predominantly of small (â¼32 kDa) soluble proteins that bind and transfer a single phospholipid, normally phosphatidylinositol or phosphatidycholine. Two forms, PITPα and PITPβ, which share approximately 80% amino acid sequence similarity, are known. Rat PITPα was labeled at specific single reactive Cys residues with I-AEDANS and used to examine PITP-membrane interactions. Upon binding to phospholipid vesicles, PITP labeled with AEDANS at the C-terminus, a region postulated to be involved in membrane binding, shows significant decreases in both steady-state and dynamic fluorescence anisotropy. In contrast, PITPs labeled with AEDANS at sites located distal to the C-terminus show increases in both steady-state and dynamic anisotropy. These results suggest that interaction of PITP with membrane surfaces leads to significant alterations in conformation and perhaps melting of the C-terminal helix.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 2, 15 December 2005, Pages 112-120
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 2, 15 December 2005, Pages 112-120
نویسندگان
Jacqueline M. Tremblay, Jay R. Unruh, Carey K. Johnson, Lynwood R. Yarbrough,