All-trans-retinoic acid and retinol binding to the FA1 site of human serum albumin competitively inhibits heme-Fe(III) association
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- 作者：Elena Di Muzioa ; Fabio Polticellia ; b ; Alessandra di Masia ; Gabriella Fanalic ; Mauro Fasanoc ; d ; Paolo Ascenzie ; ascenzi@uniroma3.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：Human serum albumin ; All-trans-retinoic acid ; Retinol ; Heme binding ; Competitive inhibition ; Molecular docking
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 January 2016
- 年：2016
- 卷：590
- 期：Complete
- 页码：56-63
- 全文大小：1878 K
文摘
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Retinoic acid and retinol bind to the FA1 site of human serum albumin.
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Retinoic acid and retinol inhibit competitively heme-Fe(III) binding to the FA1 site.
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Retinoic acid and retinol do not affect ligand binding to the FA3-FA4 cleft and the FA7 site.
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Human serum albumin and retinoic acid receptor-γ display structural similarities in recognizing retinoids.
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Human serum albumin may act as a secondary carrier of retinoic acid and retinol in human diseases.