کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1949691 | 1537781 | 2010 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The role of hydrophobic and negatively charged surface patches of lipid-free apolipoprotein A-I in lipid binding and ABCA1-mediated cholesterol efflux
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کلمات کلیدی
E. colibis(sulfosuccinimidyl) suberateBS3dMPCApoA-IABCA1LEUIPTGTrpFBSATP binding cassette transporter A1 - ATP اتصال دهنده کاست A1ATP-binding cassette transporter A1 - ATP اتصال گیرنده کاست A1Apolipoprotein A-I - آپولیپوپروتئین A-IEscherichia coli - اشریشیا کُلیisopropyl β-D-1-thiogalactopyranoside - ایزوپروپیل β-D-1-thiogalactopyranosideHis-tag - برچسب اوHistidine-tag - برچسب هیستیدینcardiovascular disease - بیماری قلب و عروقیTryptophan - تریپتوفانCVD - رسوب دهی شیمیایی بخار circular dichroism - رنگ تابی دورانیfetal bovine serum - سرم جنین گاوWavelength - طول موجFunctionality - عملکردLuria broth - لوریا بوثهLeucine - لوسینSTB - و غیره.Lipid-binding - چسبندگی لیپیدیoptical density - چگالی نوریfree cholesterol - کلسترول رایگان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Recent models of lipid-free apolipoprotein A-I, including a cross-link/homology model and an X-ray crystal structure have identified two potential functionally relevant “patches” on the protein surface. The first is a hydrophobic surface patch composed of leucine residues 42, 44, 46, and 47 and the second a negatively charged patch composed of glutamic acid residues 179, 191, and 198. To determine if these domains play a functional role, these surface patches were disrupted by site-directed mutagenesis and the bacterially expressed mutants were compared with respect to their ability to bind lipid and stimulate ABCA1-mediated cholesterol efflux. It was found that neither patch plays a significant functional role in the ability of apoA-I to accept cholesterol in an ABCA1-dependent manner, but that the hydrophobic patch did affect the ability of apoA-I to clear DMPC liposomes. Interestingly, contrary to previous predictions, disruption of the hydrophobic surface patch enhanced the lipid binding ability of apoA-I. The hydrophobic surface patch may be important to the structural stability of lipid-free apoA-I or may be a necessary permissive structural element for lipid binding.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1801, Issue 1, January 2010, Pages 64-69
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1801, Issue 1, January 2010, Pages 64-69
نویسندگان
Loren E. Smith, W. Sean Davidson,