1H, 13C, and 15N backbone chemical shift assignments of 4E-BP144–87 and 4E-BP144–87 bound to eIF4E
نویسندگان
چکیده
منابع مشابه
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 d...
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We report here the nearly complete (1)H, (15)N and (13)C resonance assignment of the La motif and RNA recognition motif 1 of human LARP6, an RNA binding protein involved in regulating collagen synthesis.
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Calcium-binding protein 1 (CaBP1) regulates inositol 1,4,5-trisphosphate receptors (InsP(3)Rs) and a variety of voltage-gated Ca(2+) channels in the brain. We report complete NMR chemical shift assignments of the Ca(2+)-saturated form of CaBP1 with Ca(2+) bound at EF1, EF3 and EF4 (residues 1-167, BMRB no. 16862).
متن کامل1H, 15N and 13C backbone chemical shift assignment of titin domains A59–A60 and A60 alone
The giant protein titin is the third most abundant protein of vertebrate striated muscle. The titin molecule is >1 μm long and spans half the sarcomere, from the Z-disk to the M-line, and has important roles in sarcomere assembly, elasticity and intracellular signaling. In the A-band of the sarcomere titin is attached to the thick filaments and mainly consists immunoglobulin-like and fibronecti...
متن کامل1H, 15N, and 13C chemical shift assignments of mouse HOXA13 DNA binding domain
The homeobox gene (HOXA13) codes for a transcription factor protein that binds to AT-rich DNA sequences and controls expression of many important proteins during embryonic morphogenesis. We report complete NMR chemical shift assignments of the mouse HOXA13 DNA binding domain (A13DBD; BMRB no. 16252).
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ژورنال
عنوان ژورنال: Biomolecular NMR Assignments
سال: 2017
ISSN: 1874-2718,1874-270X
DOI: 10.1007/s12104-017-9744-9