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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Nature structural biology

The crystal structure of the mouse apoptosis-inducing factor AIF

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature structural biology - 01 Jun 2002

Maté MJ, Ortiz-Lombardía M, Boitel B, Haouz A, Tello D, Susin SA, Penninger J, Kroemer G, Alzari PM

Link to Pubmed [PMID] – 11967568

Nat. Struct. Biol. 2002 Jun;9(6):442-6

Mitochondria play a key role in apoptosis due to their capacity to release potentially lethal proteins. One of these latent death factors is cytochrome c, which can stimulate the proteolytic activation of caspase zymogens. Another important protein is apoptosis-inducing factor (AIF), a flavoprotein that can stimulate a caspase-independent cell-death pathway required for early embryonic morphogenesis. Here, we report the crystal structure of mouse AIF at 2.0 A. Its active site structure and redox properties suggest that AIF functions as an electron transferase with a mechanism similar to that of the bacterial ferredoxin reductases, its closest evolutionary homologs. However, AIF structurally differs from these proteins in some essential features, including a long insertion in a C-terminal beta-hairpin loop, which may be related to its apoptogenic functions.

http://www.ncbi.nlm.nih.gov/pubmed/11967568