Molecular architecture of the copper-transporting ATPase ATP7B

Svetlana Lutsenko, Samuel Jayakanthan, Oleg Y. Dmitriev

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the transport of copper across the cell membranes. These activities are central to main physiological functions of ATP7B: the maintenance of copper homeostasis and synthesis of active ceruloplasmin. The other domains of ATP7B are used for regulation: using these structural elements, ATP7B responds to changing copper concentration in the cytoplasm and other signaling events. In this review, we summarize the available structural information on ATP7B and relate, whenever possible, the structural features of ATP7B to its function and regulation.

Original languageEnglish (US)
Title of host publicationClinical and Translational Perspectives on WILSON DISEASE
PublisherElsevier
Pages33-43
Number of pages11
ISBN (Electronic)9780128105320
ISBN (Print)9780128105337
DOIs
StatePublished - Jan 1 2018

Keywords

  • A domain
  • ATP7B structure
  • Metal-binding domains
  • N domain
  • Nuclear magnetic resonance spectroscopy (NMR spectroscopy)
  • P domain

ASJC Scopus subject areas

  • Medicine(all)

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