کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10759524 | 1050425 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE)
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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
![عکس صفحه اول مقاله: Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE) Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE)](/preview/png/10759524.png)
چکیده انگلیسی
S100A6 is involved in several vital biological functions, such as calcium sensing and cell proliferation. It is a homodimeric protein that belongs to the S100 protein family. The receptor for advanced glycation end products (RAGE) has been shown to play a role in the progression of various disease conditions, such as diabetes and immune/inflammatory disorders. Information regarding the association of RAGE with S100 proteins at a molecular level is useful to understand the diversity of the RAGE signaling pathways. In this report, biomolecular NMR techniques were utilized for the resonance assignment of the C3S mutation in human S100A6 and characterizing its interaction with the RAGE V domain. Further binding affinity between S100A6m and the RAGE V domain was determined by isothermal titration calorimetric studies. HADDOCK was used to generate a heterotetramer model of the S100A6m-RAGE V domain complex. This model provides an important insights into the S100-RAGE cellular signaling pathway.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 2, 3 May 2013, Pages 328-333
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 2, 3 May 2013, Pages 328-333
نویسندگان
Sepuru K. Mohan, Arun A. Gupta, Chin Yu,