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

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Bibtex

@article{fdad36cc943b4ada8339bd3cbc61da06,
title = "Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.",
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 = "Sigurbj{\"o}rg Rutardottir and Elena Karnaukhova and Chanin Nantasenamat and Napat Songtawee and Virapong Prachayasittikul and Mohsen Rajabi and {Wester Rosenl{\"o}f}, Lena and Alayash, {Abdu I} and Bo {\AA}kerstr{\"o}m",
note = "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)",
year = "2016",
doi = "10.1016/j.bbapap.2015.10.002",
language = "English",
volume = "1864",
pages = "29--41",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "1",

}