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

Paolo Ascenzi; Mauro Fasano

doi:10.1016/j.bpc.2010.03.001

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

Paolo Ascenzi, Mauro Fasano

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	16-22
Number of pages	7
Journal	Biophysical Chemistry
Volume	148
Issue number	1-3
DOIs	https://doi.org/10.1016/j.bpc.2010.03.001
Publication status	Published - May 2010

Keywords

Allostery
Drug binding
Heme binding
Heme-based reactivity
Human serum albumin

ASJC Scopus subject areas

Biochemistry
Biophysics
Organic Chemistry

Access to Document

10.1016/j.bpc.2010.03.001

Fingerprint Dive into the research topics of 'Allostery in a monomeric protein: The case of human serum albumin'. Together they form a unique fingerprint.

Cite this

@article{e6479446c7fa4767a5a8d90adbc66422,

title = "Allostery in a monomeric protein: The case of human serum albumin",

abstract = "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.",

keywords = "Allostery, Drug binding, Heme binding, Heme-based reactivity, Human serum albumin",

author = "Paolo Ascenzi and Mauro Fasano",

year = "2010",

month = may,

doi = "10.1016/j.bpc.2010.03.001",

language = "English",

volume = "148",

pages = "16--22",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier",

number = "1-3",

}

TY - JOUR

T1 - Allostery in a monomeric protein

T2 - The case of human serum albumin

AU - Ascenzi, Paolo

AU - Fasano, Mauro

PY - 2010/5

Y1 - 2010/5

N2 - 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.

AB - 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.

KW - Allostery

KW - Drug binding

KW - Heme binding

KW - Heme-based reactivity

KW - Human serum albumin

UR - http://www.scopus.com/inward/record.url?scp=77951977240&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951977240&partnerID=8YFLogxK

U2 - 10.1016/j.bpc.2010.03.001

DO - 10.1016/j.bpc.2010.03.001

M3 - Article

C2 - 20346571

AN - SCOPUS:77951977240

VL - 148

SP - 16

EP - 22

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 1-3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this