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1.
Deubiquitinases (DUBs) reversibly remove ubiquitin tags from polypeptides and play crucial regulatory roles in multiple cellular processes. Ubiquitin-specific protease 28 (Usp28), a member of the DUB family, exerts its deubiquitination function on key protein molecules in a couple of cancer-associated pathways, likely acting as an oncogenic factor in vivo. The N-terminal ubiquitin-binding domains (UBDs) of Usp28 are potentially required for the full catalytic capacity of Usp28 toward ubiquitin chains. Here we report the expression, purification and 1H, 13C and 15N backbone and side-chain resonance assignments of the N-terminal UBDs of Usp28. The BMRB accession number is 19077. 相似文献
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Chung-Kyung Lee Kwon Joo Yeo Eunha Hwang Hae-Kap Cheong 《Biomolecular NMR assignments》2013,7(1):89-92
Angiogenin is an unusual member of the pancreatic ribonuclease superfamily that induces formation of new blood vessels and is a promising anti-cancer target. Here we report backbone and side chain 1H, 13C, and 15N resonance assignments for rat angiogenin (residues 24–145), excluding the N-terminal signal peptide. These data allow nuclear magnetic resonance structure and inhibitor-binding studies with the aim of providing angiogenin antagonists as potential therapeutics. 相似文献
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Chengyan Wu Jing Hong Xinli Liao Chenyun Guo Xueji Wu Hongyu Hu Donghai Lin 《Biomolecular NMR assignments》2013,7(1):105-108
CcmG is a periplasmic, membrane-anchored protein widely distributed in a variety of species. In Escherichia coli, the CcmG protein always acts as a weak reductant in the electron transport chain during cytochrome c maturation (Ccm). Here we report 1H, 15N and 13C backbone and side-chain resonance assignments of the reduced CcmG protein (residues 19–185, renumbered as 1–167) from E. coli. This work lays the essential basis for the further structural and functional analysis of reduced CcmG. 相似文献
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Raf-1 kinase inhibitor protein (RKIP) plays a pivotal role in modulating multiple signaling networks. Here we report backbone
and side chain resonance assignments of uniformly 15N, 13C labeled human RKIP. 相似文献
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Cuiping Fu Yu Peng Xinli Liao Chenyun Guo Donghai Lin 《Biomolecular NMR assignments》2013,7(2):155-158
AK1 (Adenylate Kinase 1) plays crucial roles in processes such as cellular phosphotransfer networks, neuronal maturation and regeneration, gating of ABC transporter CFTR, tumor cell metabolism and myocardial energetic homeostasis. Here we report 1H, 15N and 13C backbone and side-chain resonance assignments of the human AK1 protein in apo form. This work lays the essential basis for the further structure determination of hAK1. 相似文献
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Lipocalin2 plays an important role in the innate immune system. In this article we report the backbone and side-chain resonance
assignments of rat lipocalin2 (rLcn2). These assignments provide a basis for determining the structure and dynamics of rLcn2.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. 相似文献
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David A. Yadin Ian B. Robertson Sacha A. Jensen Penny A. Handford Christina Redfield 《Biomolecular NMR assignments》2014,8(1):75-80
Fibrillins are extracellular, disulphide-rich glycoproteins that form 10–12 nm diameter microfibrils in connective tissues. They are found in the majority of higher animals, from jellyfish to humans. Fibrillin microfibrils confer properties of elasticity and strength on connective tissue and regulate growth factor availability in the extracellular matrix (ECM). Mutations in FBN1, the human gene encoding the fibrillin-1 isoform, are linked to several inherited connective tissue disorders. The fibrillin-1 N-terminus forms many functionally-important interactions, both with other fibrillin molecules and various ECM components. In particular, the first four domains, the fibrillin unique N-terminal (FUN) and three epidermal growth factor (EGF)-like domains (FUN-EGF3), are implicated in microfibril assembly and growth factor sequestration. The structure of these domains, which comprise 134 residues, is unknown. We have produced a recombinant fragment corresponding to this region of human fibrillin-1. Here, we report 1H, 13C and 15N resonance assignments of the FUN-EGF3 fragment. Assignments will facilitate structure determination, analysis of interdomain dynamics and the mapping of interaction surfaces. 相似文献
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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. 相似文献
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The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing
of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. SARS-CoV Mpro is composed of a catalytic N-terminal domain and an α-helical C-terminal domain linked by a long loop. Even though the N-terminal
domain of SARS-CoV Mpro adopts a similar chymotrypsin-like fold as that of piconavirus 3C protease, the extra C-terminal domain is required for SARS-CoV
Mpro to be enzymatically active. Here, we reported the NMR assignments of the SARS-CoV Mpro N-terminal domain alone, which are essential for its solution structure determination. 相似文献
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Edwige B. Garcin Olivier Bornet Laetitia Pieulle Françoise Guerlesquin Corinne Sebban-Kreuzer 《Biomolecular NMR assignments》2010,4(2):135-137
Based on sequence homology, desulfothioredoxin (DTrx) from Desulfovibrio vulgaris Hildenborough has been identified as a new member of the thioredoxin superfamily. Desulfothioredoxin (104 amino acids) contains a particular active site consensus sequence, CPHC probably correlated to the anaerobic metabolism of these bacteria. We report the full 1H, 13C and 15N resonance assignments of the reduced and the oxidized form of desulfothioredoxin (DTrx). 2D and 3D heteronuclear NMR experiments were performed using uniformly 15N-, 13C-labelled DTrx. More than 98% backbone and 96% side-chain 1H, 13C and 15N resonance assignments were obtained. (BMRB deposits with accession number 16712 and 16713). 相似文献
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Norovirus protease cleaves the virus-encoded polyprotein into six mature nonstructural proteins, presenting itself as an essential
enzyme for the viral replication as well as an attractive target for the antiviral drug development. A deeper understanding
of the structural mechanism of the protease-substrates/inhibitors interactions by means of solution NMR methods would facilitate
a rational design of the virus protease inhibitor. We here report the backbone and side-chain resonance assignment of the
protease from Norwalk virus, which is the prototype strain of norovirus. The assignment data has been deposited in the BMRB
database under the accession number 17523. 相似文献
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Hop/STI1 (Hsp-organizing protein/stress-induced-phosphoprotein 1) is a molecular co-chaperone, which coordinates Hsp70 and Hsp90 activity during client protein folding through interactions with its TPR1 and TPR2A domains. Hsp90 substrates include a diverse set of proteins, many of which have been implicated in tumorigenesis. Over-expression of Hsp90 in cancer cells stabilizes mutant oncoproteins promoting cancer cell survival. Disruption of Hsp90 and its co-chaperone machinery has become a promising strategy for the treatment of cancer. STI1 has also been described as a neurotrophic signaling molecule through its interactions with the prion protein (PrPC). Here, we report the 1H, 13C and 15N backbone assignments of the TPR1 and TPR2A domains of mouse STI1, which interact with Hsp70 and Hsp90, respectively. 1H-15N HSQC spectra of TPR2A domain in the presence of a peptide encoding the C-terminal Hsp90 binding site revealed significant chemical shift changes indicating complex formation. These results will facilitate the screening of potential molecules that inhibit STI1 complex formation with Hsp70 and/or Hsp90 for the treatment of cancer and detailed structural studies of the STI1-PrPC complex. 相似文献
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Grondin JM Chitayat S Ficko-Blean E Boraston AB Smith SP 《Biomolecular NMR assignments》2012,6(2):139-142
The Gram-positive anaerobe Clostridium perfringens is an opportunistic bacterial pathogen that secretes a battery of enzymes involved in glycan degradation. These glycoside hydrolases are thought to be involved in turnover of mucosal layer glycans, and in the spread of major toxins commonly associated with the development of gastrointestinal diseases and gas gangrene in humans. These enzymes employ multi-modularity and carbohydrate-binding function to degrade extracellular eukaryotic host sugars. Here, we report the full (1)H, (15)N and (13)C chemical shift resonance assignments of the first family 32 carbohydrate-binding module from NagH, a secreted family 84 glycoside hydrolase. 相似文献
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Chromatin-remodeling proteins have a pivotal role in normal cell function and development, catalyzing conformational changes in DNA that ultimately result in changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 (CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of which contain two chromo domains and an ATP-dependent helicase module. CHD3, CHD4 and CHD5 also contain two contiguous PHD domains and have an extended N-terminal region that has not previously been characterized. We have identified a stable domain in the N-terminal region of CHD4 and report here the backbone and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB No. 18906). 相似文献
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YopH is a protein tyrosine phosphatase that functions as a required virulence factor in Yersinia. Here we report the backbone resonance assignments for a point mutant of the C-terminal catalytic domain of YopH. 相似文献