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Biomolecular NMR Assignments

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https://www.readbyqxmd.com/read/29332151/1h-13c-and-15n-backbone-and-partial-side-chain-resonance-assignments-of-the-c-terminal-domain-of-hiv-1-pr55gag-encompassed-in-ncp15
#1
Valéry Larue, Marjorie Catala, Anissa Belfetmi, Loussiné Zargarian, Olivier Mauffret, Carine Tisné
During HIV-1 assembly, the Pr55Gag polyprotein precursor (Gag) interacts with the genomic RNA, with lipids of the plasma membrane, with host proteins (ALIX, TSG101) through the ESCRT complex, with the viral protein Vpr and are involved in intermolecular interactions with other Pr55Gag proteins. This network of interactions is responsible for the formation of the viral particle, the selection of genomic RNA and the packaging of Vpr. The C-terminal domain of Gag encompassed in NCp15 is involved in the majority of these interactions, either by its nucleocapsid or its p6 domains...
January 13, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29327103/1h-13c-and-15n-resonance-assignments-of-nedd8-from-trypanosoma-brucei
#2
Rui Wang, Jiahai Zhang, Shanhui Liao, Xiaoming Tu
Neural precursor cell-expressed, developmently downregulated 8 (NEDD8) is a small ubiquitin-like modifier, which plays important roles in many cellular processes. Although it has been well studied in many eukaryotes, NEDD8 is still uncharacterized in some unicellular parasites, such as Trypanosoma brucei (T. brucei). Here we report the resonance assignments of NEDD8 from T. brucei.
January 11, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29327102/chemical-shift-assignments-of-retinal-degeneration-3-protein-rd3
#3
Sunghyuk Lim, Diana Cudia, Qinhong Yu, Igor Peshenko, Alexander M Dizhoor, James B Ames
Retinal degeneration 3 protein (RD3) binds to retinal membrane guanylyl cyclase (RetGC) and suppresses the basal activity of RetGC in photoreceptor cells that opposes the allosteric activation of the cyclase by GCAP proteins. Mutations in RD3 that disrupt its inhibition of RetGC are implicated in human retinal degenerative disorders. Here we report both backbone and sidechain NMR assignments for the RD3 protein (BMRB accession no. 27305).
January 11, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29318533/chemical-shift-assignments-of-chu_1110-an-ahsa1-like-protein-from-cytophaga-hutchinsonii
#4
Chunjie Liang, Ting He, Tao Li, Yunhuang Yang, Jiang Zhu, Maili Liu
AHSA1 protein family is one of the four largest families in the Bet v1-like protein superfamily. The functions and structures of proteins in AHSA1 family are still largely unknown. CHU_1110 with 167 amino acids and a molecular weight of 19.2 kDa is a member of the AHSA1 family from Cytophaga hutchinsonii, a soil bacterium known for its ability to digest crystalline cellulose. Here we report the complete 1H, 13C and 15N chemical shift assignments of CHU_1110. The secondary structural elements of CGL2373 are consistent with the canonical AHSA1 structure...
January 9, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29313214/backbone-and-side-chain-chemical-shift-assignments-of-the-kringle-domain-of-human-receptor-tyrosine-kinase-like-orphan-receptor-1-ror1
#5
Xiaofang Ma, Yingying Zhang, Bin Liu, Jiahui Yang, Kaifeng Hu
Receptor tyrosine kinase-like orphan receptor 1 (ROR1) expresses at high level in many cancers and has been suggested as a potential therapeutic target. It was reported that the Kringle (KNG) domain of ROR1 extracellular region is involved in ROR1/ROR2 heterooligomerization. Monoantibodies that target KNG domain of ROR1 could induce apoptosis of chronic lymphocytic leukemia cells. Here we present the backbone and side chain assignments of KNG domain of ROR1, which lays a foundation for its further structural and function research...
January 8, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29299752/backbone-resonance-assignment-of-the-response-regulator-protein-phobnf20d-from-escherichia-coli
#6
Xinhui Kou, Xinghong Liu, Yixiang Liu, Conggang Li, Maili Liu, Ling Jiang
PhoB is a response regulator of the PhoR/PhoB two-component signal transduction system that is involved in the regulation of the phosphate (Pho) regulon of Escherichia coli. PhoB has two domains, receiver domain and effector domain. The receiver domain can be phosphorylated by its cognate histidine kinase PhoR and the phosphorylation induces conformational changes of the full length protein of PhoB that promote the DNA binding and transcription. Three-dimensional crystal structures of PhoB receiver domain (PhoBN) have been solved under apo or BeF3- (a phosphoryl analog) binding forms and it has been found that PhoBN is dimerized in both situations...
January 3, 2018: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29280056/assignment-of-1h-13c-and-15n-resonances-and-secondary-structure-of-the-rgd1-rhogap-domain
#7
Denis Martinez, Valérie Prouzet-Mauléon, Michel Hugues, François Doignon, Benoît Odaert
The protein Rgd1 is involved in the regulation of cytoskeleton formation and in signalling pathways that control cell polarity and growth in Saccharomyces cerevisiae. Rgd1p is composed of a F-BAR domain required for membrane binding and a RhoGAP domain responsible for activating Rho3p and Rho4p, two GTPases respectively involved in bud growth and cytokinesis. Rgd1p is recruited to the membrane through interactions with phosphoinositide lipids, which bind the two isolated domains and stimulate the RhoGAP activity on Rho4p...
December 26, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29224116/chemical-shift-assignments-of-the-partially-deuterated-fyn-sh2-sh3-domain
#8
Fabien Kieken, Karine Loth, Nico van Nuland, Peter Tompa, Tom Lenaerts
Src Homology 2 and 3 (SH2 and SH3) are two key protein interaction modules involved in regulating the activity of many proteins such as tyrosine kinases and phosphatases by respective recognition of phosphotyrosine and proline-rich regions. In the Src family kinases, the inactive state of the protein is the direct result of the interaction of the SH2 and the SH3 domain with intra-molecular regions, leading to a closed structure incompetent with substrate modification. Here, we report the 1H, 15N and 13C backbone- and side-chain chemical shift assignments of the partially deuterated Fyn SH3-SH2 domain and structural differences between tandem and single domains...
December 9, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29189986/1h-13c-and-15n-chemical-shift-assignments-of-a-g-quadruplex-forming-sequence-within-the-kras-proto-oncogene-promoter-region
#9
Julien Marquevielle, M V Vasantha Kumar, Jean-Louis Mergny, Gilmar F Salgado
Single stranded guanine rich DNA (or RNA) sequences adopt noncanonical secondary structures called G-quadruplexes (G4). Functionally, quadruplexes control gene transcription and regulate activities such as replication, gene recombination or alternative splicing. Hence they are potential targets for cancer, neuronal, and viral related diseases. KRAS is one of the most mutated oncogenes in the genome of cancer cells and contains a nuclease hypersensitive element (NHE) sequence capable of forming G-quadruplexes via its six runs of guanines...
November 30, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29168057/-1-h-15-n-and-13-c-backbone-resonance-assignments-of-pentaerythritol-tetranitrate-reductase-from-enterobacter-cloacae-pb2
#10
Andreea I Iorgu, Nicola J Baxter, Matthew J Cliff, Jonathan P Waltho, Sam Hay, Nigel S Scrutton
Pentaerythritol tetranitrate reductase (PETNR) is a flavoenzyme possessing a broad substrate specificity and is a member of the Old Yellow Enzyme family of oxidoreductases. As well as having high potential as an industrial biocatalyst, PETNR is an excellent model system for studying hydrogen transfer reactions. Mechanistic studies performed with PETNR using stopped-flow methods have shown that tunneling contributes towards hydride transfer from the NAD(P)H coenzyme to the flavin mononucleotide (FMN) cofactor and fast protein dynamics have been inferred to facilitate this catalytic step...
November 22, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29090418/chemical-shift-assignment-of-a-thermophile-frataxin
#11
Masooma Rasheed, Robert Yan, Geoff Kelly, Annalisa Pastore
Frataxin is the protein responsible for the genetically-inherited neurodegenerative disease Friedreich's ataxia caused by partial silencing of the protein and loss of function. Although the frataxin function is not yet entirely clear, it has been associated to the machine that builds iron-sulfur clusters, essential prosthetic groups involved in several processes and is strongly conserved in organisms from bacteria to humans. Two of its important molecular partners are the protein NFS1 (or IscS in bacteria), that is the desulfurase which converts cysteine to alanine and produces sulfur, and ISU (or IscU), the scaffold protein which transiently accepts the cluster...
October 31, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29086898/-1-h-13-c-and-15-n-resonance-assignments-of-fas1-iv-domain-of-human-periostin-a-component-of-extracellular-matrix-proteins
#12
Hyosuk Yun, Eun-Hee Kim, Chul Won Lee
Periostin, an extracellular matrix protein, is secreted by fibroblasts and is overexpressed in various types of cancers. The four internal repeat fasciclin 1 (FAS1) domains of human periostin play crucial roles in promoting tumor metastasis and progression via interaction with cell surface integrins. Among four FAS1 domains of human periostin, the fourth FAS1 domain (FAS1-IV) was prepared for NMR study, since only FAS1-IV was highly soluble, and showed a well-dispersed 2D (1)H-(15)N HSQC spectrum. Here, we report nearly complete backbone and side chain resonance assignments and a secondary structural analysis of the FAS1-IV domain as first steps toward the structure determination of FAS1-IV of human periostin...
October 31, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29071576/nmr-assignments-of-the-n-terminal-signaling-domain-of-the-tonb-dependent-outer-membrane-transducer-pupb
#13
Jaime L Jensen, Qiong Wu, Christopher L Colbert
Outer membrane TonB-dependent transducers (TBDTs) actively transport ferric siderophore complexes from the extracellular environment into Gram-negative bacteria. They also participate in a cell-surface signaling regulatory pathway that results in upregulation of the transducer itself, in response to iron-deplete conditions. The TBDT PupB transports ferric pseudobactin, and signals through its N-terminal signaling domain (NTSD), while the TBDT homolog PupA is signaling-inactive. Here, we report the NMR chemical shift assignments of the PupB-NTSD...
October 25, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29067546/-1-h-13-c-and-15-n-chemical-shift-assignment-of-lissencephaly-1-homology-lish-domain-homodimer-of-human-two-hybrid-associated-protein-1-with-ranbpm-twa1
#14
Talita S de Araujo, Marcius S Almeida
The CTLH complex is a large, highly conserved eukaryotic complex composed of eight proteins that has been associated to several cellular functions, more often described as an E3 ubiquitin ligase complex involved in protein degradation through ubiquitination but also via vacuole-dependent degradation. A common feature observed in several components of this complex is the presence of the domains lissencephaly-1 homology (LisH) and C-terminal to LisH (CTLH). The LisH domain is found in several proteins involved in chromosome segregation, microtubule dynamics, and cell migration...
October 24, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29064000/-1-h-15-n-13-c-backbone-resonance-assignment-of-the-c-terminal-domain-of-enzyme-i-from-thermoanaerobacter-tengcongensis
#15
Rochelle Rea Dotas, Vincenzo Venditti
Phosphoenolpyruvate binding to the C-terminal domain (EIC) of enzyme I of the bacterial phosphotransferase system (PTS) initiates a phosphorylation cascade that results in sugar translocation across the cell membrane and controls a large number of essential pathways in bacterial metabolism. EIC undergoes an expanded to compact conformational equilibrium that is regulated by ligand binding and determines the phosphorylation state of the overall PTS. Here, we report the backbone (1)H, (15)N and (13)C chemical shift assignments of the 70 kDa EIC dimer from the thermophilic bacterium Thermoanaerobacter tengcongensis...
October 24, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29063999/backbone-1-h-13-c-and-15-n-resonance-assignments-of-the-ob-domain-of-the-single-stranded-dna-binding-protein-hssb2-nabp1-obfc2a-and-chemical-shift-mapping-of-the-dna-binding-interface
#16
Ruvini Kariawasam, Maddison Knight, Roland Gamsjaeger, Liza Cubeddu
Single stranded DNA-binding proteins (SSBs) are essential for the maintenance of genome integrity and are required in in all known cellular organisms. Over the last 10 years, the role of two new human SSBs, hSSB1 (NABP2/OBFC2B) and hSSB2 (NABP1/OBFC2A), has been described and characterised in various important DNA repair processes. Both these proteins are made up of a conserved oligonucleotide-binding (OB) fold that is responsible for ssDNA recognition as well a unique flexible carboxy-terminal extension involved in protein-protein interactions...
October 24, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29030803/-1-h-13-c-and-15-n-backbone-resonance-assignments-of-the-%C3%AE-lactamase-blap-from-bacillus-licheniformis-749-c-and-two-mutational-variants
#17
David Thorn, Jennifer Kay, Noureddine Rhazi, Mireille Dumoulin, Alessandra Corazza, Christian Damblon
Class A β-lactamases have been widely used as versatile scaffolds to create hybrid (or chimeric) proteins for a series of applications ranging from basic research to medicine. We have, in particular, used the β-lactamase BlaP from Bacillus licheniformis 749/C (BlaP) as a protein scaffold to create model polyglutamine (polyQ) proteins in order to better understand the mechanism(s) by which an expanded polyQ sequence triggers the formation of amyloid fibrils. The model chimeras were designed by inserting a polyQ sequence of various lengths at two different locations within BlaP (i...
October 13, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/28980143/nmr-assignments-of-the-n-terminal-domain-of-staphylococcus-aureus-hibernation-promoting-factor-sahpf
#18
Konstantin S Usachev, Rustam Kh Ayupov, Shamil Z Validov, Iskander Sh Khusainov, Marat M Yusupov
Staphylococcus aureus: hibernation-promoting factor (SaHPF) is a 22.2 kDa stationary-phase protein that binds to the ribosome and turns it to the inactive form favoring survival under stress. Sequence analysis has shown that this protein is combination of two homolog proteins obtained in Escherichia coli-ribosome hibernation promoting factor (HPF) (11,000 Da) and ribosome modulation factor RMF (6500 Da). Binding site of E. coli HPF on the ribosome have been shown by X-ray study of Thermus thermophilus ribosome complex...
October 4, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/28866776/-1-h-15-n-13-c-backbone-resonance-assignments-of-human-phosphoglycerate-kinase-in-a-transition-state-analogue-complex-with-adp-3-phosphoglycerate-and-magnesium-trifluoride
#19
Zhalgas Serimbetov, Nicola J Baxter, Matthew J Cliff, Jonathan P Waltho
Human phosphoglycerate kinase (PGK) is an energy generating glycolytic enzyme that catalyses the transfer of a phosphoryl group from 1,3-bisphosphoglycerate (BPG) to ADP producing 3-phosphoglycerate (3PG) and ATP. PGK is composed of two α/β Rossmann-fold domains linked by a central α-helix and the active site is located in the cleft formed between the N-domain which binds BPG or 3PG, and the C-domain which binds the nucleotides ADP or ATP. Domain closure is required to bring the two substrates into close proximity for phosphoryl transfer to occur, however previous structural studies involving a range of native substrates and substrate analogues only yielded open or partly closed PGK complexes...
October 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/28856584/-1-h-15-n-and-13-c-resonance-assignments-of-ixolaris-a-tissue-factor-pathway-inhibitor-from-the-tick-salivary-gland
#20
V S De Paula, F H S Silva, I M B Francischetti, R Q Monteiro, A P Valente
Ixolaris is a two-Kunitz tick salivary gland protein identified in Ixodes scapularis that presents sequence homology to TFPI (tissue factor pathway inhibitor). It binds to the coagulation enzyme factor Xa (FXa) or to its zymogen form, FX, and further inhibits tissue factor/FVIIa complex (extrinsic Xnase compex). Differently from TFPI, Ixolaris does not bind to the active site cleft of FXa. Instead, complex formation is mediated by the FXa heparin-binding exosite, which may also results in decreased FXa activity into the prothrombinase complex...
October 2017: Biomolecular NMR Assignments
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