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1.
Human regenerating (Reg) genes belong to the C-type lectin superfamily and express secretory proteins in various tissues. Reg Iα, also named lithostathine, has multiple roles in numerous biological events such as cytokines, anti-apoptotic factors and the calcium carbonate crystals inhibitor. Under physiological pH, Reg Iα becomes largely insoluble after a self-proteolysis process, and the N-terminally truncated form readily polymerizes into fibrils, which leads to neurodegenerative diseases. Reg Iα may form protofibril via lateral hydrophobic interactions with a native-like conformation. The structural basis from the native to fibril form, as well as the carbohydrate binding sites on Reg Iα, remain unknown. Here we present the NMR backbone and side-chain assignments of Reg Iα for use in further NMR investigations. 相似文献
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Alexey Yu. Denisov Pekka Maattanen Tara Sprules David Y. Thomas Kalle Gehring 《Biomolecular NMR assignments》2007,1(1):129-130
Protein disulfide isomerase (PDI) participates in protein folding and catalyses formation of disulfide bonds. The b′ domain of human PDI contributes to binding unfolded proteins; its structure is stabilized by the b domain. Here, we report NMR chemical shift assignments for the bb′ fragment. 相似文献
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The ζ-COP is one subunit of the COP I coatomer, which mediates the protein trafficking from the cis-Golgi complex to the endoplasmic
reticulum and also functions in the intra-Golgi trafficking. The NMR assignments of the ζ-COP are essential for its solution
structure determination. 相似文献
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NOXO1 (Nox Organizer 1) is a homolog of the NAPDH oxidase protein p47
phox
. NADPH oxidases transfer electrons from NADPH to molecular oxygen, generating the superoxide anion. NOXO1 contains an N-terminal
PX (phox homology) domain and is one of several PX domain-containing proteins found in the cytosolic subunits of the NADPH
oxidase complex. These PX domains bind to membrane lipids and target the protein to membranes, recruiting other cytosolic
components to the membrane bound components and aiding formation of a active enzyme complex. This recruitment represents a
level of regulation of these oxidases. Here we report the backbone assignments of NOXO1β PX. 相似文献
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As part of our NMR structure determination of the human Interleukin-1α, we report nearly complete NMR chemical shift assignments for the 1H, 13C and 15N nuclei. 相似文献
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Critical to the use of solution NMR to describe the structure and flexibility of membrane proteins is the thorough understanding of the degree of perturbation induced by the detergent or other membrane mimetic. To develop a deeper understanding of the interaction between membrane proteins and micelles or bicelles, we will investigate the differences in structure and flexibility of a model membrane protein TM0026 from Thermotoga maritima using solution NMR. A comparison of the structural differences between TM0026 solubilized in different detergent combinations will provide important insight into the degree of modulation of membrane proteins by detergent physical properties. Here we report the nearly complete backbone and Cβ resonance assignments of the two transmembrane helical model protein TM0026. These assignments are the first step to using TM0026 to elucidate the interaction between membrane proteins and membrane mimetics. 相似文献
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Yin C Aramini JM Ma LC Cort JR Swapna GV Krug RM Montelione GT 《Biomolecular NMR assignments》2011,5(2):215-219
Human interferon-stimulated gene 15 protein (ISG15), also called ubiquitin cross-reactive protein (UCRP), is the first identified
ubiquitin-like protein containing two ubiquitin-like domains fused in tandem. The active form of ISG15 is conjugated to target
proteins via the C-terminal glycine residue through an isopeptide bond in a manner similar to ubiquitin. The biological role
of ISG15 is strongly associated with the modulation of cell immune function, and there is mounting evidence suggesting that
many viral pathogens evade the host innate immune response by interfering with ISG15 conjugation to both host and viral proteins
in a variety of ways. Here we report nearly complete backbone 1HN, 15N, 13C′, and 13Cα, as well as side chain 13Cβ, methyl (Ile-δ1, Leu, Val), amide (Asn, Gln), and indole N–H (Trp) NMR resonance assignments for the 157-residue human ISG15
protein. These resonance assignments provide the basis for future structural and functional solution NMR studies of the biologically
important human ISG15 protein. 相似文献
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Lin TH Huang YC Chin ML Chen YC Jeng HH Lin FM Shiao MS Horiuchi A Greengard P Nairn AC Huang HB 《Journal of biomolecular NMR》2004,28(4):413-414
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Iren Wang Yuan-Chao Lou Yu-Ching Lin Shih-Chi Lo Alan Yueh-Luen Lee Shih-Hsiung Wu Chinpan Chen 《Biomolecular NMR assignments》2007,1(2):201-203
The small α-domain of Lon protease is thought to carry the substrate-recognition, nucleotide-binding, and DNA-binding sites.
Here we report the complete resonance assignment of the α-domain for Bacillus subtilis Lon protease (Bs-Lon α-domain). 相似文献
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Mark Jeeves Darren M. McClelland Alastair J. Barr Michael Overduin 《Biomolecular NMR assignments》2008,2(2):101-103
PTPN7 is a protein tyrosine phosphatase responsible for inactivation of MAPK in leukocytes. Here we report the backbone resonance
assignments of the 34 kDa phosphatase domain of human PTPN7, which is amplified in myeloid malignancies and deleted in lymphoproliferative
disorders. 相似文献
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Zhongzheng Yang Jie Shen Xu Zhang Cody Vild Wenxian Lan Maili Liu Zhaohui Xu Chunyang Cao 《Biomolecular NMR assignments》2013,7(2):331-334
Vta1 and Vps60 are two ESCRT associated proteins, their direct interaction enhances Vps4 ATPase activity. The N-terminal domain of Vta1 (residues 1–167aa, named as Vta1NTD) contains two tandem MIT domains, which specifically recognize Vps60 and Did2 but not other ESCRT-III subunits. The fragment Vps60 (128–186aa) was reported to display full activity of Vps60, which stimulates Vps4 ATPase in a Vta1-dependent manner. To study the structural basis for the interaction between Vta1 and Vps60, as a first step, here, we report the resonance assignments of the sequential backbone atoms and the side chains of the residues in the two components of Vta1NTD/Vps60128–186 complex at pH 7.0 and 20 °C (BMRB No. 18521). 相似文献
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Nyon MP Kirkpatrick J Cabrita LD Christodoulou J Gooptu B 《Biomolecular NMR assignments》2012,6(2):153-156
Alpha(1)-antitrypsin is a 45-kDa (394-residue) serine protease inhibitor synthesized by hepatocytes, which is released into the circulatory system and protects the lung from the actions of neutrophil elastase via a conformational transition within a dynamic inhibitory mechanism. Relatively common point mutations subvert this transition, causing polymerisation of α(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of α(1)-antitrypsin using multidimensional heteronuclear NMR spectroscopy. These assignments provide the starting point for a detailed solution state characterization of the structural properties of this highly dynamic protein via NMR methods. 相似文献
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