Solution Structure of the COMMD1 N-terminal Domain

Monika Sommerhalter, Yongbo Zhang, Amy C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

COMMD1 is the prototype of a new protein family that plays a role in several important cellular processes, including NF-κB signaling, sodium transport, and copper metabolism. The COMMD proteins interact with one another via a conserved C-terminal domain, whereas distinct functions are predicted to result from a variable N-terminal domain. The COMMD proteins have not been characterized biochemically or structurally. Here, we present the solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108). This domain adopts an α-helical structure that bears little resemblance to any other helical protein. The compact nature of N-COMMD1 suggests that full-length COMMD proteins are modular, consistent with specific functional properties for each domain. Interactions between N-COMMD1 and partner proteins may occur via complementary electrostatic surfaces. These data provide a new foundation for biochemical characterization of COMMD proteins and for probing COMMD1 protein-protein interactions at the molecular level.

Original languageEnglish (US)
Pages (from-to)715-721
Number of pages7
JournalJournal of Molecular Biology
Volume365
Issue number3
DOIs
StatePublished - Jan 19 2007

Keywords

  • COMMD1
  • COMMD6
  • MURR1
  • NF-κB
  • Wilson disease protein

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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