1H, 13C, and 15N chemical shift assignments of ZCCHC9

ZCCHC9 is a human nuclear protein with sequence homology to yeast Air1p/Air2p proteins which are RNA-binding subunits of the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex involved in nuclear RNA quality control and degradation in yeast. The ZCCHC9 protein contains four retroviral-type zinc knuckle motifs. Here, we report the NMR spectral assignment of the zinc knuckle region of ZCCHC9. These data will allow performing NMR structural and RNA-binding studies of ZCCHC9 with the aim to investigate its role in the RNA quality control in human.     

1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin

As part of our NMR structure determination of the palladin Ig3 domain, we report nearly complete NMR chemical shift assignments for the ¹H, ¹³C, and ¹⁵N nuclei.     

1H, 13C,and 15N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65

Phosphotyrosine binding domains (PTB) are protein–protein interaction domains that play important roles in various cellular signal transduction pathways. The second phosphotyrosine binding domain (PTB2) of the human scaffolding protein FE65 interacts with the C-terminal part of the Amyloid Precursor Protein (APP) involved in Alzheimer’s disease. The structure of PTB2 in complex with a 32 amino acid fragment of APP has been solved previously by X-ray crystallography. Here, we report the NMR spectral assignments of the free FE65 PTB2. This provides the basis for further investigation of the interactions of PTB2 with peptides and small organic ligands with the aim of disrupting the PTB2-APP interaction.     

1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG

The human ether à go-go related gene (hERG) voltage-gated potassium controls the rapid delayed rectifier potassium current (I_ks) in heart. The N-terminal 135 amino acids (NTD) form a Per-Arnt-Sim (PAS) domain which involves in signal transduction and protein–protein interactions. NTD was shown to be necessary for the regulation of the channel activity through its interaction with the channel pore region of hERG. Mutations in NTD were related to serious heart diseases. We report the ¹H, ¹³C and ¹⁵N chemical shift assignments for NTD using 2D and 3D heteronuclear NMR experiments. More than 95% backbone resonance assignments were obtained.     

1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1)

Tensin is an important cytoplasmic phosphoprotein localized to integrin-mediated focal adhesion. It links actin cytoskeleton to extracellular matrix through its N-terminal actin-binding domain and C-terminal phosphotyrosine-binding domain. Studies of knockout mice revealed the critical roles of tensin in skeletal muscle regeneration, renal function and regulation of cell migration. The SH2 domain of tensin interacts with various tyrosine-phosphorylated proteins thus functions as a platform for dis/assembly of signaling molecules. It has also been implicated in recruiting a tumor supperssor protein DLC1 (deleted in live cancer 1) to the focal adhesion, which is required for oncogenic inhibition effect of DLC1 in a phosphotyrosine-independent manner. Here, we report complete chemical shift assignments of the SH2 domain of human tensin2 determined by triple resonance experiments. The resonance assignments serve as a basis for our further functional studies and structure determination by NMR spectroscopy. (BMRB deposits with accession number 16472).     

1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain

Cell adhesion molecules play a crucial role in fundamental biological processes via regulating cell–cell interactions. Nerve injury induced protein1 (Ninjurin1) is a novel adhesion protein that has no significant homology with other known cell adhesion molecules. Here we present the assignment of an 81 aa construct for human Ninjurin1 Extracellular N-Terminal (ENT) domain, which comprises the critical adhesion domain.     

1H, 15N,and 13C chemical shift assignments of murine calcium-binding protein 4

Calcium-binding protein 4 (CaBP4) regulates voltage-gated Ca²⁺ channels in retinal rod cells and specific mutations within CaBP4 are associated with congenital stationary night blindness type 2. We report complete NMR chemical shift assignments of the Ca²⁺-saturated form of CaBP4 with Ca²⁺ bound at EF1, EF3 and EF4 (BMRB no. 18877).     

1H, 13C and 15N chemical shift assignments for the N-terminal PAS domain of the KCNH channel from Zebrafish

The KCNH channels are voltage-gated potassium channels that play important roles in heart and nerve cells. The N-terminal region of the KCNH channel contains a Per-Arnt-Sim (PAS) domain which is important for the channel gating through interaction with other regions of the channel. To study the solution structure of the N-terminal PAS domain of the KCNH channel from Zebrafish (zNTD), we over-expressed and purified zNTD. We report the resonance assignments for zNTD. The data will allow us to perform structural studies for this domain, which will provide insight into its structural basis for the molecular interaction with other regions of the KCNH channel.     

1H, 15N, and 13C chemical shift assignments of calcium-binding protein 1 (CaBP1)

Calcium-binding protein 1 (CaBP1) regulates inositol 1,4,5-trisphosphate receptors (InsP₃Rs) and a variety of voltage-gated Ca²⁺ channels in the brain. We report complete NMR chemical shift assignments of Ca²⁺-free CaBP1 (residues 1–167, BMRB no. 15197).     

1H, 13C and 15N resonance assignments of human H-REV107 N-terminal domain

Human H-REV107 protein is the representative of a novel class II tumor suppressor family, which is lost in tumor cells and can induce cell death after restoration. The NMR assignments of the H-REV107 N-terminal domain are essential for its solution structure determination.     

1H, 13C,and 15N chemical shift assignments of neuronal calcium sensor protein,hippocalcin

Hippocalcin, a member of the neuronal calcium sensor (NCS) subclass of the calmodulin superfamily, serves as an important calcium sensor for the slow afterhyperpolarizing (sAHP) current in the hippocampus, which underlies some forms of learning and memory. Hippocalcin is also a calcium sensor for hippocampal long-term depression (LTD) and genetically linked to neurodegenerative diseases. We report NMR chemical shift assignments of Ca²⁺-free hippocalcin (BMRB no. 18627).     

1H, 13C and 15N resonance assignments of the pyrin domain from human PYNOD

PYNOD is a novel protein belonging to a large family of proteins containing the nucleotide-binding and oligomerization domain (NOD) involved in inflammation and apoptosis. Human PYNOD inhibits inflammatory response mediated by caspase-1 and apoptosis-associated speck-like protein containing a caspase-recruitment domain (ASC). Here we report the ¹H, ¹³C and ¹⁵N resonance assignments and secondary structure identification of the pyrin domain (PYD) of human PYNOD as the first step towards elucidating the structural basis of the anti-inflammatory activity of PYNOD.     

1H, 13C, and 15N chemical shift assignments for the RNA recognition motif of Nab3

Nuclear polyadenylated RNA-binding (Nab)3 protein is an RNA-binding protein that is involved in the poly(A) independent termination pathway. Here, we report the NMR spectral assignments of RNA-recognition motif (RRM) of Nab3. The assignment will allow performing NMR structural and RNA-binding studies of Nab3 with the aim to investigate its role in the poly(A) independent termination pathway.     

1H, 15N, and 13C chemical shift assignments of calcium-bound calcium-binding protein 1 (CaBP1)

Calcium-binding protein 1 (CaBP1) regulates inositol 1,4,5-trisphosphate receptors (InsP₃Rs) and a variety of voltage-gated Ca²⁺ channels in the brain. We report complete NMR chemical shift assignments of Ca²⁺-bound CaBP1 (residues 1–167, BMRB no. 15623).     

1H, 15N, and 13C chemical shift assignments of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei

Flagellar calcium binding proteins are expressed in a variety of trypanosomes and are potential drug targets for Chagas disease and African sleeping sickness. We report complete NMR chemical shift assignments of the flagellar calcium binding protein calflagin Tb24 of Trypanosoma brucei. (BMRB no. 18011).