umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2017 (English)In: Biometals, ISSN 0966-0844, E-ISSN 1572-8773, Vol. 30, no 6, p. 823-840Article, review/survey (Refereed) Published
Abstract [en]

Wilson Disease (WD) is a hereditary genetic disorder, which coincides with a dysfunctional copper (Cu) metabolism caused by mutations in ATP7B, a membrane-bound P-1B-type ATPase responsible for Cu export from hepatic cells. The N-terminal part (similar to 600 residues) of the multi-domain 1400-residue ATP7B constitutes six metal binding domains (MBDs), each of which can bind a copper ion, interact with other ATP7B domains as well as with different proteins. Although the ATP7B's MBDs have been investigated in vitro and in vivo intensively, it remains unclear how these domains modulate overall structure, dynamics, stability and function of ATP7B. The presence of six MBDs is unique to mammalian ATP7B homologs, and many WD causing missense mutations are found in these domains. Here, we have summarized previously reported in vitro biophysical data on the MBDs of ATP7B and WD point mutations located in these domains. Besides the demonstration of where the research field stands today, this review showcasts the need for further biophysical investigation about the roles of MBDs in ATP7B function. Molecular mechanisms of ATP7B are important not only in the development of new WD treatment but also for other aspects of human physiology where Cu transport plays a role.

Place, publisher, year, edition, pages
Springer, 2017. Vol. 30, no 6, p. 823-840
Keyword [en]
Wilson disease, ATP7B, Atox1, Metal-binding domains, Cu transport, Disease-causing mutations
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-142450DOI: 10.1007/s10534-017-0058-2ISI: 000415283000001PubMedID: 29063292OAI: oai:DiVA.org:umu-142450DiVA, id: diva2:1162657
Available from: 2017-12-05 Created: 2017-12-05 Last updated: 2018-06-09Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Authority records BETA

Li, YaozongWittung-Stafshede, Pernilla

Search in DiVA

By author/editor
Li, YaozongWittung-Stafshede, Pernilla
By organisation
Department of Chemistry
In the same journal
Biometals
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 61 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf