NMR-driven secondary and tertiary structure model of Ca2+-loaded calexcitin.

Biochem Biophys Res Commun

Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Ont., Canada M5G 1L7.

Published: May 2006


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Calexcitin (CE) is a Ca2+-binding protein which is expressed in neuronal cells and is a member of the sarcoplasmic Ca2+-binding protein subfamily. The peptide backbone of Ca2+-CE has been assigned by NMR and it shows that CE is composed of nine alpha-helices-forming four EF-hands and an additional helix near the C-terminus. A structural model of CE suggests the presence of a putative recessed hydrophobic pocket that may be involved in Ca2+-mediated protein-ligand interactions. This feature is unique to CE and is absent in other SCPs, such as those from Branchiostoma and Nereis, and from calerythrin.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bbrc.2006.02.182DOI Listing

Publication Analysis

Top Keywords

ca2+-binding protein
8
nmr-driven secondary
4
secondary tertiary
4
tertiary structure
4
structure model
4
model ca2+-loaded
4
ca2+-loaded calexcitin
4
calexcitin calexcitin
4
calexcitin ca2+-binding
4
protein expressed
4

Similar Publications

The environment surrounding plants is far from stable, compelling the plant to perceive and adapt to numerous biotic and abiotic constraints, including insect attacks. The perception of a feeding insect typically entails the identification of herbivore-associated molecular patterns causing a sequential increase in cytosolic Ca levels. Calmodulin-like proteins (CMLs) are Ca sensor proteins with conserved EF-hands, which decode Ca signals to generate a stress-specific response.

View Article and Find Full Text PDF

Titin is the third contractile filament in the sarcomere, and it plays a critical role in sarcomere integrity and both passive and active tension. Unlike the thick and thin filaments, which are polymers of myosin and actin, respectively, titin is a single protein that spans from Z-disk to M-line. The N2A region within titin has been identified as a signaling hub for the muscle and is shown to be involved in multiple interactions.

View Article and Find Full Text PDF

To encode continuous sound stimuli, the inner hair cell (IHC) ribbon synapses utilize calcium-binding proteins (CaBPs), which reduce the inactivation of their Ca1.3 calcium channels. Mutations in the gene underlie non-syndromic autosomal recessive hearing loss DFNB93.

View Article and Find Full Text PDF

Introduction: Anti-MDA5-positive dermatomyositis (anti-MDA5-DM) is a rare autoimmune disease that often leads to rapid-progressive interstitial lung disease (RP-ILD). The lack of effective prediction and treatment methods makes RP-ILD a major risk factor for death in patients with this condition. S100A6 is a member of the S100 Ca2 + - binding protein family, which plays important roles in inflammation, tumor, injury, and fibroblast reparation.

View Article and Find Full Text PDF

Comprehensive Characterization of a Subfamily of Ca-Binding Proteins in Mouse and Human Retinal Neurons at Single-Cell Resolution.

eNeuro

September 2024

Oujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision and Brain Health), Wenzhou 325000, China

Ca-binding proteins (CaBPs; CaBP1-5) are a subfamily of neuronal Ca sensors with high homology to calmodulin. Notably, CaBP4, which is exclusively expressed in rod and cone photoreceptors, is crucial for maintaining normal retinal functions. However, the functional roles of CaBP1, CaBP2, and CaBP5 in the retina remain elusive, primarily due to limited understanding of their expression patterns within inner retinal neurons.

View Article and Find Full Text PDF