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Tsuruta T Goda N Umetsu Y Iwaya N Kuwahara Y Hiroaki H 《Biomolecular NMR assignments》2012,6(1):23-25
Stomatin, a 288-residue protein, is a component of the membrane skeleton of red blood cells (RBCs), which helps to physically
support the membrane and maintains its function. In RBCs, stomatin binds to the glucose transporter GLUT-1 and may regulate
its function. Stomatin has a stomatin/prohibitin/flotillin/HflK (SPFH) domain at the center of its polypeptide chain. There
are 12 SPFH domain-containing proteins, most of which are localized at the cellular or subcellular membranes. Although the
molecular function of the SPFH domain has not yet been established, the domain may be involved in protein oligomerization.
The SPFH domain of the archaeal stomatin homolog has been shown to form unique oligomers. Here we report the 15N, 13C, and 1H chemical shift assignments of the SPFH domain of human stomatin [hSTOM(SPFH)]. These may help in determining the structure
of hSTOM(SPFH) in solution as well as in clarifying its involvement in protein oligomerization. 相似文献
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Czajlik A Thompson GS Khan GN Kalverda AP Homans SW Trinick J 《Biomolecular NMR assignments》2012,6(1):39-41
Single molecules of the giant protein titin extend across half of the muscle sarcomere, from the Z-line to the M-line, and
have roles in muscle assembly and elasticity. In the A-band titin is attached to thick filaments and here the domain arrangement
occurs in regular patterns of eleven called the large super-repeat. The large super-repeat itself occurs eleven times and
forms nearly half the titin molecule. Interactions of the large super-repeats with myosin are consistent with a role in thick
filament assembly. Here we report backbone assignments of the titin A67-A68 domain tandem (Fn-Ig) from the third super-repeat
(A65-A75) completed using triple resonance NMR experiments. 相似文献
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Hidenori Ohnishi Hidehito Tochio Zenichiro Kato Takeshi Kimura Hidekazu Hiroaki Naomi Kondo Masahiro Shirakawa 《Biomolecular NMR assignments》2010,4(2):123-125
Myeloid differentiating factor 88 (MyD88) is one of a critical adaptor molecule in the Toll-like receptor (TLR) signaling pathway. The TIR domain of MyD88 serves as a protein–protein interaction module and interacts with other TIR-containing proteins such as Mal (MyD88 adaptor-like) and Toll-like receptor 4 to form signal initiation complexes. Here we report the 15N, 13C, and 1H chemical shift assignments of the TIR domain of MyD88. The resonance assignments obtained in this work will contribute to the study of heteromeric TIR–TIR interactions between MyD88 and TIR-containing receptors or adaptors. 相似文献
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Melanie Schwarten Carsten Berghaus Rolf Heumann Raphael Stoll 《Biomolecular NMR assignments》2007,1(1):105-108
Ras homologue enriched in brain (Rheb) is a small GTPase that plays an important role in tuberous sclerosis. Here we present
the backbone assignments of activated rRheb in complex with the non-hydrolisable GTP analogue GppNHp. These assignments now
provide a basis for the analysis of rRheb’s interaction with putative effectors in order to further elucidate the physiological
function of this GTPase and its role in the regulation of neuronal cell volume as well as in tuberous sclerosis. 相似文献
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1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor. 总被引:1,自引:0,他引:1 下载免费PDF全文
W. J. Fairbrother M. A. Champe H. W. Christinger B. A. Keyt M. A. Starovasnik 《Protein science : a publication of the Protein Society》1997,6(10):2250-2260
Nearly complete sequence-specific 1H, 13C, and 15N resonance assignments are reported for the backbone atoms of the receptor-binding domain of vascular endothelial growth factor (VEGF), a 23-kDa homodimeric protein that is a major regulator of both normal and pathological angiogenesis. The assignment strategy relied on the use of seven 3D triple-resonance experiments [HN(CO)CA, HNCA, HNCO, (HCA)CONH, HN(COCA)HA, HN(CA)HA, and CBCA-(CO)NH] and a 3D 15N-TOCSY-HSQC experiment recorded on a 0.5 mM (12 mg/mL) sample at 500 MHz, pH 7.0, 45 degrees C. Under these conditions, 15N relaxation data show that the protein has a rotational correlation time of 15.0 ns. Despite this unusually long correlation time, assignments were obtained for 94 of the 99 residues; 8 residues lack amide 1H and 15N assignments, presumably due to rapid exchange of the amide 1H with solvent under the experimental conditions used. The secondary structure of the protein was deduced from the chemical shift indices of the 1H alpha, 13C alpha, 13C beta, and 13CO nuclei, and from analysis of backbone NOEs observed in a 3D 15N-NOESY-HSQC spectrum. Two helices and a significant amount of beta-sheet structure were identified, in general agreement with the secondary structure found in a recently determined crystal structure of a similar VEGF construct [Muller YA et al., 1997, Proc Natl Acad Sci USA 94:7192-7197]. 相似文献
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Kai U. Cormann Masahiko Ikeuchi Matthias Rögner Marc M. Nowaczyk Raphael Stoll 《Biomolecular NMR assignments》2009,3(2):247-249
Photosystem II (PSII) is a large membrane protein complex that uses light to split water into molecular oxygen, protons, and
electrons. Here we report the 1H, 15N and 13C backbone chemical shift assignments for the Psb27 protein of Photosystem II from Synechocystis PCC 6803. These assignments will now provide the basis for the structural analysis of the Psb27 protein. 相似文献
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The 1H, 13C, and 15N backbone resonance assignments have been made for the Src homology 2 (SH2) domain of the human molecular adapter protein Grb14. The assignments, along with the majority of the non-aromatic side-chain 1H and 13C resonances are reported. The SH2 domain has been complexed with a phosphotyrosine-containing peptide (pY766) corresponding to the putative binding site in the fibroblast growth factor receptor (FGFR1). Chemical shift changes upon binding are also reported. 相似文献
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Carsten Berghaus Melanie Schwarten Rolf Heumann Raphael Stoll 《Biomolecular NMR assignments》2007,1(1):45-47
Rheb (Ras homologue enriched in brain) is a small GTPase that plays an important role in tuberous sclerosis. Here we present
the backbone assignments of rRheb in its GDP-bound state. These assignments now provide a basis for the analysis of the interaction
of rRheb with putative factors in order to elucidate the function of this GTPase and its role in the MAP kinase pathway of
neuronal cells and in tuberous sclerosis. 相似文献
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Zorzini V Haesaerts S Cheung A Loris R van Nuland NA 《Biomolecular NMR assignments》2011,5(2):157-160
MazF proteins are ribonucleases that cleave mRNA with high sequence-specificity as part of bacterial stress response and that
are neutralized by the action of the corresponding antitoxin MazE. Prolonged activation of the toxin MazF leads to cell death.
Several mazEF modules from Gram-negative bacteria have been characterized in terms of catalytic activity, auto-regulation mechanism and
structure, but less is known about their distant relatives found in Gram-positive organisms. Currently, no solution NMR structure
is available for any wild-type MazF toxin. Here we report the 1H, 15N and 13C backbone and side-chain chemical shift assignments of this toxin from the pathogen bacterium Staphylococcus aureus. The BMRB accession number is 17288. 相似文献