کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2051243 | 1074195 | 2006 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site](/preview/png/2051243.png)
چکیده انگلیسی
We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa. However, substitution of residues C-terminal to helix D (R132 and K133) to Ala had minimal effect on heparin affinity but resulted in appreciable activation. We conclude that charge neutralization or reversal in the heparin binding site does not drive the activating conformational change of AT, and that the role of helix D elongation is to stabilize the activated state.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 19, 21 August 2006, Pages 4709-4712
Journal: FEBS Letters - Volume 580, Issue 19, 21 August 2006, Pages 4709-4712
نویسندگان
Jonathan Langdown, Wendy J. Carter, Trevor P. Baglin, James A. Huntington,