PDBsum entry 2e6w

Metal binding protein

PDB id: 2e6w

Contents

Protein chain

96 a.a. *

Metals

_CA ×2

* Residue conservation analysis

PDB id:

2e6w

Name:

Metal binding protein

Title:

Solution structure and calcium binding properties of ef-hands 3 and 4 of calsenilin

Structure:

Calsenilin. Chain: a. Fragment: ef-hands 3 and 4. Synonym: dre-antagonist modulator, dream, kv channel-interacting protein 3, kchip3, a-type potassium channel modulatory protein 3. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dream, kchip3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

1 models

Authors:

L.Yu,C.Sun,R.Mendoza,E.Hebert,A.Pereda-Lopez,P.J.Hajduk, E.T.Olejniczak

Key ref:

L.Yu et al. (2007). Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin. Protein Sci, 16, 2502-2509. PubMed id: 17962406 DOI: 10.1110/ps.072928007

Date:

05-Jan-07 Release date: 27-Nov-07

Protein chain

Q9Y2W7  (CSEN_HUMAN) -  Calsenilin from Homo sapiens

Seq: 256 a.a.

Struc: 96 a.a.

DOI no: 10.1110/ps.072928007

Protein Sci 16:2502-2509 (2007)

PubMed id: 17962406

Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin.

L.Yu, C.Sun, R.Mendoza, J.Wang, E.D.Matayoshi, E.Hebert, A.Pereda-Lopez, P.J.Hajduk, E.T.Olejniczak.

ABSTRACT

Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling.

Selected figure(s)

Figure 6.
Figure 6. Molecular surfaces of calsenilin EF3--4 colored by local

Figure 7.
Figure 7. Ribbon plots comparing the structures of calsenilin EF3--4 (red)

The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 2502-2509) copyright 2007.

Figures were selected by an automated process.