Allostery in a monomeric protein: The case of human serum albumin

被引：164

作者：

Ascenzi, Paolo ^{[1
,2
]}

Fasano, Mauro ^{[3
,4
]}

机构：

[1] Univ Roma Tre, Dept Biol & Interdepartmental Lab, Lab Electron Microscopy, I-00146 Rome, Italy

[2] Natl Inst Infect Dis IRCCS Lazzaro Spallanzani, Rome, Italy

[3] Univ Insubria, Dept Struct & Funct Biol, Busto Arsizio, VA, Italy

[4] Univ Insubria, Ctr Neurosci, Busto Arsizio, VA, Italy

来源：

BIOPHYSICAL CHEMISTRY | 2010年 / 148卷 / 1-3期

关键词：

Allostery; Drug binding; Heme-based reactivity; Heme binding; Human serum albumin; FAMILIAL DYSALBUMINEMIC HYPERTHYROXINEMIA; SITE-DIRECTED MUTAGENESIS; IRON PROTOPORPHYRIN-IX; ACID-BINDING SITES; ANTI-HIV DRUGS; NITRIC-OXIDE; HEME-ALBUMIN; CRYSTALLOGRAPHIC ANALYSIS; STRUCTURAL BASIS; LIGAND-BINDING;

D O I：

10.1016/j.bpc.2010.03.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins. Here, both functional and structural aspects of the allosteric modulation of heme and drug (e.g., warfarin and ibuprofen) binding to HSA and of the drug-dependent reactivity of HSA-heme are reviewed. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：16 / 22

页数：7

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