Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8148501
- author
- Rutardottir, Sigurbjörg LU ; Karnaukhova, Elena ; Nantasenamat, Chanin ; Songtawee, Napat ; Prachayasittikul, Virapong ; Rajabi, Mohsen ; Wester Rosenlöf, Lena LU ; Alayash, Abdu I and Åkerström, Bo LU
- organization
- publishing date
- 2016
- 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}}, }