Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture.


Journal Article

Copper is essential for biological processes such as free radical detoxification, mitochondrial respiration and iron metabolism. A central player in copper homeostasis is the high-affinity integral plasma membrane copper transporter Ctr1. However, the precise mechanisms by which Ctr1 functions are not known. Here, we highlight an important breakthrough in our understanding of how Ctr1 facilitates Cu(I) movement across membranes: the publication of structural details for human Ctr1 obtained from 2D crystallography and electron microscopy.

Full Text

Duke Authors

Cited Authors

  • Nose, Y; Rees, EM; Thiele, DJ

Published Date

  • November 2006

Published In

Volume / Issue

  • 31 / 11

Start / End Page

  • 604 - 607

PubMed ID

  • 16982196

Pubmed Central ID

  • 16982196

International Standard Serial Number (ISSN)

  • 0968-0004

Digital Object Identifier (DOI)

  • 10.1016/j.tibs.2006.09.003


  • eng

Conference Location

  • England