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

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

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

Yasuhiro Nose,Erin M Rees,Dennis J Thiele,

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.

Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture. Publishing Authors By Initials

Y Nose,EM Rees,DJ Thiele,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation research

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Trends in biochemical sciences

VOLUME: 31

Page Numbers: 604-7

Journal Abbreviation: Trends Biochem. Sci.

ISSN: 0968-0004

DAY: 18

MONTH: 09

YEAR: 2006

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

Number of References:

LANGUAGE: eng

NlmUniqueID: 7610674

Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture. Keywords Mesh Terms:

KEYWORDS: Protein Conformation

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture. Information

Substance Name: Copper

Registry Number: 7440-50-8

Grant and Affiliation Information for Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture.

AFFILIATION: Department of Pharmacology and Cancer Biology, Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Research Drive-LSRC C351, Durham, NC 27710-3813, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM41840

ACRONYM: GM

MEDLINETA: Trends Biochem Sci

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