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Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.

Rutardottir, Sigurbjörg LU ; Karnaukhova, Elena ; Nantasenamat, Chanin ; Songtawee, Napat ; Prachayasittikul, Virapong ; Rajabi, Mohsen ; Wester Rosenlöf, Lena LU ; Alayash, Abdu I and Åkerström, Bo LU (2016) In Biochimica et Biophysica Acta - Proteins and Proteomics 1864(1). p.29-41
Abstract
α1-Microglobulin (A1M) is a reductase and radical scavenger involved in physiological protection against oxidative damage. These functions were previously shown to be dependent upon cysteinyl-, C34, and lysyl side-chains, K(92, 118,130). A1M binds heme and the crystal structure suggests that C34 and H123 participate in a heme binding site. We have investigated the involvement of these five residues in the interactions with heme.
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochimica et Biophysica Acta - Proteins and Proteomics
volume
1864
issue
1
pages
29 - 41
publisher
Elsevier
external identifiers
  • pmid:26497278
  • scopus:84946606197
  • wos:000370464300004
  • pmid:26497278
ISSN
1570-9639
DOI
10.1016/j.bbapap.2015.10.002
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (BMC) (013024020), Faculty of Medicine (000022000), Medical Inflammation Research (013212019)
id
fdad36cc-943b-4ada-8339-bd3cbc61da06 (old id 8148501)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26497278?dopt=Abstract
date added to LUP
2016-04-01 13:26:22
date last changed
2022-04-06 05:10:08
@article{fdad36cc-943b-4ada-8339-bd3cbc61da06,
  abstract     = {{α1-Microglobulin (A1M) is a reductase and radical scavenger involved in physiological protection against oxidative damage. These functions were previously shown to be dependent upon cysteinyl-, C34, and lysyl side-chains, K(92, 118,130). A1M binds heme and the crystal structure suggests that C34 and H123 participate in a heme binding site. We have investigated the involvement of these five residues in the interactions with heme.}},
  author       = {{Rutardottir, Sigurbjörg and Karnaukhova, Elena and Nantasenamat, Chanin and Songtawee, Napat and Prachayasittikul, Virapong and Rajabi, Mohsen and Wester Rosenlöf, Lena and Alayash, Abdu I and Åkerström, Bo}},
  issn         = {{1570-9639}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{29--41}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta - Proteins and Proteomics}},
  title        = {{Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.}},
  url          = {{http://dx.doi.org/10.1016/j.bbapap.2015.10.002}},
  doi          = {{10.1016/j.bbapap.2015.10.002}},
  volume       = {{1864}},
  year         = {{2016}},
}