کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10758148 | 1050404 | 2013 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein-protein interfaces
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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
Lipocalin α1-microglobulin (α1M) is a conserved glycoprotein present in plasma and in the interstitial fluids of all tissues. α1M is linked to a heterogeneous yellow-brown chromophore of unknown structure, and interacts with several target proteins, including α1-inhibitor-3, fibronectin, prothrombin and albumin. To date, there is little knowledge about the interaction sites between α1M and its partners. Here, we report the crystal structure of the human α1M. Due to the crystallization occurring in a low ionic strength solution, the unidentified chromophore with heavy electron density is observed at a hydrophobic inner tube of α1M. In addition, two conserved surface regions of α1M are proposed as putative protein-protein interface sites. Further study is needed to unravel the detailed information about the interaction between α1M and its partners.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 439, Issue 3, 27 September 2013, Pages 346-350
Journal: Biochemical and Biophysical Research Communications - Volume 439, Issue 3, 27 September 2013, Pages 346-350
نویسندگان
Yangli Zhang, Zengqiang Gao, Zhen Guo, Hongpeng Zhang, Zhenzhen Zhang, Miao Luo, Haifeng Hou, Ailong Huang, Yuhui Dong, Deqiang Wang,