Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1

Matthew Turner, David E. Anderson, Sahana Rajan, Johannes W Hell, James B. Ames

Research output: Contribution to journalArticle

Abstract

The regulation and localization of the neuronal voltage gated Ca2+ channel CaV1.2 is important for synaptic plasticity associated with learning and memory. The cytoskeletal protein, α-actinin-1 is known to interact with CaV1.2 and stabilize its localization at the postsynaptic membrane. Here we report both backbone and sidechain NMR assignments for the C-terminal EF-hands (EF3 and EF4) of α-actinin-1 (residues 824–892, called ACTN_EF34) bound to the IQ-motif (residues 1644–1665) from CaV1.2 (BMRB accession no. 25902).

Original languageEnglish (US)
Pages (from-to)219-222
Number of pages4
JournalBiomolecular NMR Assignments
Volume10
Issue number1
DOIs
StatePublished - Apr 1 2016

Fingerprint

EF Hand Motifs
Actinin
Chemical shift
Neuronal Plasticity
Cytoskeletal Proteins
Plasticity
Nuclear magnetic resonance
Learning
Membranes
Data storage equipment
Electric potential

Keywords

  • Ca1.2
  • EF-hand
  • IQ-motif
  • Long-term depression
  • Synaptic plasticity
  • α-Actinin-1

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1. / Turner, Matthew; Anderson, David E.; Rajan, Sahana; Hell, Johannes W; Ames, James B.

In: Biomolecular NMR Assignments, Vol. 10, No. 1, 01.04.2016, p. 219-222.

Research output: Contribution to journalArticle

Turner, Matthew ; Anderson, David E. ; Rajan, Sahana ; Hell, Johannes W ; Ames, James B. / Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1. In: Biomolecular NMR Assignments. 2016 ; Vol. 10, No. 1. pp. 219-222.
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