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

Sigurbjörg Rutardottir, Elena Karnaukhova, Chanin Nantasenamat, Napat Songtawee, Virapong Prachayasittikul, Mohsen Rajabi, Lena Wester Rosenlöf, Abdu I Alayash, Bo Åkerström

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)29-41
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1864
Issue number1
DOIs
Publication statusPublished - 2016

Bibliographical 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)

Subject classification (UKÄ)

  • Cell and Molecular Biology

Fingerprint

Dive into the research topics of 'Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.'. Together they form a unique fingerprint.

Cite this