3u9j
From Proteopedia
Crystal structure of oxidized human FBXL5 hemerythrin like domain
Structural highlights
Function[FBXL5_HUMAN] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.[1] [2] [3] Publication Abstract from PubMedIron sensing: The F-box and leucine-rich repeat containing protein FBXL5 is an iron sensor that regulates the ubiquitination of iron regulatory protein IRP2. Crystal structures of the iron-sensing hemetrythrin (Hr)-like domain of human FBXL5 (FBXL5 Hr) were determined in oxidized and reduced states. These structures revealed the mechanisms of iron sensing by FBXL5. The Structural Basis of Iron Sensing by the Human F-box Protein FBXL5.,Shu C, Sung MW, Stewart MD, Igumenova TI, Tan X, Li P Chembiochem. 2012 Apr 16;13(6):788-91. doi: 10.1002/cbic.201200043. PMID:22492618[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Human | Large Structures | Li, P | Fbox | Iron sensor | Lrr | Protein binding | Ubiquitin ligase e3
