کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10759425 | 1050422 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism
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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
We observed that the BBA73 protein exists as a homodimer both in the crystal and in solution. The monomers interact with their N-terminal α-helices and form a cleft that could potentially serve as a ligand or receptor binding site. To confirm that the protein dimerizes through the interaction of the N-terminal regions, we produced an N-terminal deletion mutant of BBA73 to disrupt dimerization, and we determined the crystal structure of the truncated BBA73 protein at 1.9 Ã
resolution. The truncated protein did not form a homodimer, and the crystal structure confirmed that the overall fold is identical to that of the native BBA73 protein. Notably, a paralogous protein CspA from B. burgdorferi with known crystal structure also forms a homodimer, albeit through an entirely different interaction between the monomers.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 4, 17 May 2013, Pages 848-853
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 4, 17 May 2013, Pages 848-853
نویسندگان
Kalvis Brangulis, Ivars Petrovskis, Andris Kazaks, Viesturs Baumanis, Kaspars Tars,