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

Research output: Contribution to journalArticle

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.

Details

Authors
  • Sigurbjörg Rutardottir
  • Elena Karnaukhova
  • Chanin Nantasenamat
  • Napat Songtawee
  • Virapong Prachayasittikul
  • Mohsen Rajabi
  • Lena Wester Rosenlöf
  • Abdu I Alayash
  • Bo Åkerström
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cell and Molecular Biology
Original languageEnglish
Pages (from-to)29-41
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1864
Issue number1
Publication statusPublished - 2016
Publication categoryResearch
Peer-reviewedYes

Bibliographic 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)