کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10594626 | 981836 | 2012 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
In vitro evolution of an HIV integrase binding protein from a library of C-terminal domain γS-crystallin variants
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: In vitro evolution of an HIV integrase binding protein from a library of C-terminal domain γS-crystallin variants In vitro evolution of an HIV integrase binding protein from a library of C-terminal domain γS-crystallin variants](/preview/png/10594626.png)
چکیده انگلیسی
A protein without natural binding functions was engineered to bind HIV-1 integrase. Phage display selections applied a library of variants based on the C-terminal domain of the eye lens protein human γS-crystallin. Multiple loop regions were altered to encode libraries with â3.6 Ã 1011 different variants. A crystallin variant, termed integrase binding protein-10 (IBP-10), inhibits integrase catalysis with nanomolar Ki values. IBP-10 interacts with the integrase C-terminal domain and inhibits integrase substrate affinity. This allosteric mechanism allows IBP-10 to inhibit drug-resistant integrase variants. The results demonstrate the applicability of the crystallin scaffold for the discovery of binding partners and enzyme inhibitors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 22, Issue 17, 1 September 2012, Pages 5584-5589
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 22, Issue 17, 1 September 2012, Pages 5584-5589
نویسندگان
Issa S. Moody, Shawn C. Verde, Cathie M. Overstreet, W. Jr., Gregory A. Weiss,