共查询到20条相似文献,搜索用时 31 毫秒
1.
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
2.
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
3.
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
4.
This paper describes a [15N,1H]/[13C,1H]-TROSY experiment for the simultaneous acquisition of the heteronuclear chemical shift correlations of backbone amide 15N–1H groups, side chain 15N–1H2 groups and aromatic 13C–1H groups in otherwise highly deuterated proteins. The 15N–1H and 13C–1H correlations are extracted from two subspectra of the same data set, thus preventing possible spectral overlap of aromatic and amide protons in the 1H dimension. The side-chain 15N–1H2 groups, which are suppressed in conventional [15N,1H)-TROSY, are observed with high sensitivity in the 15N–1H subspectrum. [15N,1H]/[13C,1H]-TROSY was used as the heteronuclear correlation block in a 3D [1H,1H]-NOESY-[15N,1H]/[13C,1H]-TROSY experiment with the membrane protein OmpA reconstituted in detergent micelles of molecular weight 80000 Da, which enabled the detection of numerous NOEs between backbone amide protons and both aromatic protons and side chain 15N–1H2 groups. 相似文献
5.
Julia Rumpf Bernd Simon Yvonne Groemping Michael Sattler 《Biomolecular NMR assignments》2008,2(1):55-58
EH domains are protein–protein interaction domains that function in vesicular trafficking and endocytosis. Here, we report
the NMR spectral assignments of the high-affinity complex between the second EH domain of Eps15 and a stonin 2 peptide—providing
the basis for the characterization of a two-site binding mode. 相似文献
6.
7.
1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer 总被引:1,自引:0,他引:1
Irina V. Nesmelova Mabel Pang Linda G. Baum Kevin H. Mayo 《Biomolecular NMR assignments》2008,2(2):203-205
Galectin-1 is an important regulator of leukocyte function and tumor angiogenesis. Recently, this lectin has been identified
as a molecular target for the potent angiogenesis inhibitor anginex. Here, we report 1H, 13C, and 15N chemical shift assignments for human galectin-1 as determined by using heteronuclear triple resonance NMR spectroscopy. 相似文献
8.
Lihua Liu Mengmeng Ren Peng Peng Yan Chun Lu Li Jinfeng Zhao Jingjing Fang Lixiang Peng Jijun Yan Jinfang Chu Yiqin Wang Shoujiang Yuan Xueyong Li 《遗传学报》2021,48(1):88-91
正Lateral branching is an important determinant of shoot architecture and crop yield. The plant hormone strigolactone (SL) inhibits lateral bud outgrowth in various plant species. Deficiencies in SL biosynthesis and signal transduction result in excessive outgrowth of lateral buds (Stirnberg et al., 2002; Sorefan et al., 2003). 相似文献
9.
The interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/alpha-1) is a major immunogenic component of schistosomes. It potently triggers the release of interleukin-4 from
basophilic granulocytes in an IgE-dependent manner, suggesting a key function in the modulation of the host’s immune response
to Schistosoma mansoni infection. Here we present the near complete assignment of an IPSE/alpha-1 variant, IPSEΔNLS, which comprises the core domain
of the protein. 相似文献
10.
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
11.
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
12.
Judith C. Amburgey Frits Abildgaard Mary R. Starich Sanjiv Shah Dana C. Hilt David J. Weber 《Journal of biomolecular NMR》1995,6(2):171-179
Summary The 1H, 13C and 15N NMR assignments of the backbone and side-chain resonances of rat S100 were made at pH 6.5 and 37°C using heteronuclear multidimensional NMR spectroscopy. Analysis of the NOE correlations, together with amide exchange rate and 1H, 13C and 13C chemical shift data, provided extensive secondary structural information. Thus, the secondary structure of S100 was determined to comprise four helices (Leu3-Ser18, helix I; Lys29-Leu40, helix II; Gln50-Glu62, helix III; and Phe70-Ala83, helix IV), four loops (Gly19-His25, loop I; Ser41-Glu49, loop II; Asp63-Gly66, loop III; and Cys84-Glu91, loop IV) and two -strands (Lys26-Lys28, -strand I and Glu67-Asp69, -strand II). The -strands were found to align in an antiparallel manner to form a very small -sheet. This secondary structure is consistent with predictions that S100 contains two helix-loop-helix Ca2+-binding motifs known as EF-hands. The alignment of the -sheet, which brings the two EF-hand domains of S100 into close proximity, is similar to that of several other Ca2+ ion-binding proteins. 相似文献
13.
Daiwen Yang Ronald A. Venters Geoffrey A. Mueller W.Y. Choy Lewis E. Kay 《Journal of biomolecular NMR》1999,14(4):333-343
HNCO-based 3D pulse schemes are presented for measuring 1HN-15N,15N-13CO, 1HN-13CO,13CO-13C and 1HN-13C dipolar couplings in 15N,13C,2-labeled proteins. The experiments are based on recently developed TROSY methodology for improving spectral resolution and sensitivity. Data sets recorded on a complex of Val, Leu, Ile (1 only) methyl protonated 15N,13C,2H-labeled maltose binding protein and -cyclodextrin as well as 15N,13C,2H-labeled human carbonic anhydrase II demonstrate that precise dipolar couplings can be obtained on proteins in the 30–40 kDa molecular weight range. These couplings will serve as powerful restraints for obtaining global folds of highly deuterated proteins. 相似文献
14.
We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin
and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its
solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone
variants will advance understanding of cataract formation. 相似文献
15.
16.
Sujoy Mukherjee Simon P. Pondaven Nicole Höfer Christopher P. Jaroniec 《Biomolecular NMR assignments》2009,3(2):255-259
1H, 13C and 15N resonance assignments are presented for a recombinant 114 amino acid human immunoglobulin (Ig) κIV light-chain variable
domain (VL) LEN, which displays a high degree of sequence identity with another human Ig κIV VL, SMA. While SMA is highly amyloidogenic in vivo and in vitro and has been linked to the pathogenesis of light-chain amyloidosis,
LEN is non-amyloidogenic in vivo and can be converted to the amyloid state only in vitro under destabilizing conditions. Measurements
of longitudinal and transverse amide 15N relaxation rates confirm that, as expected, LEN is a dimer at physiological pH and typical concentrations used for NMR studies,
and the analysis of secondary chemical shifts indicates that the protein has a high β-sheet content. These findings are consistent
with previously published biophysical data and the high-resolution X-ray structure of LEN. 相似文献
17.
Pavel Macek Lukáš Žídek Michaela Rumlová Iva Pichová Vladimír Sklenář 《Biomolecular NMR assignments》2008,2(1):43-45
Mason-Pfizer monkey virus (M-PMV) belongs to the family of betaretroviruses characterized by the assembly of immature particles
within cytoplasm of infected cells in contrast to other retroviruses (e.g. HIV, RSV) that assemble their immature particles
at a plasma membrane. Simultaneously with or shortly after budding a virus-encoded protease is activated and the Gag polyprotein
is cleaved into three major structural proteins: matrix (MA), capsid (CA), and nucleocapsid (NC) protein. Mature retroviral
CA proteins consist of two independently folded structural domains: N-terminal domain (NTD) and C-terminal dimerization domain
(CTD), separated by a flexible linker. As a first step toward the solution structure elucidation, we present nearly complete
backbone and side-chain 1H, 15N and 13C resonance assignment of the M-PMV NTD CA. 相似文献
18.
Aline C. Simon Peter J. Simpson William Hawthorne Lisa R. Hale Rachael M. Goldstone Rivka L. Isaacson 《Biomolecular NMR assignments》2013,7(2):271-274
The first stage of the GET (guided entry of tail-anchored proteins) mechanism for tail-anchored (TA) membrane protein insertion is thought to occur when Sgt2 (small, glutamine-rich, tetratricopeptide repeat-containing protein 2) binds TA proteins upon their release from the ribosome. It sorts them and passes the majority over to a complex of Get5 and Get4 for transmission along the GET pathway and delivery to their membrane destination. Sgt2 is a 38 kDa protein consisting of three domains. The N-terminal domain effects tight dimerisation of the protein and is also the site for binding with the ubiquitin-like (UBL) domain of Get5. Here we have expressed and purified uniformly-15N/13C-labelled N-terminal Sgt2 (Sgt2_NT) and its binding partner, Get5 UBL domain (Get5_UBL) and assigned the backbone and side-chain resonances as a basis for structure solution of the individual components and, ultimately, the complex. This will provide detailed molecular insight into the early stages of the GET pathway. 相似文献
19.
Shovanlal Gayen Subramanian Vivekanandan Goran Biuković Gerhard Grüber Ho Sup Yoon 《Biomolecular NMR assignments》2007,1(1):23-25
Energy coupling between the A1 ATPase of archaea type A1AO ATP synthase and its integral membrane sub-complex AO occurs via the stalk part, formed by the subunits C, D and F. To provide a molecular basis of the energy coupling, we performed
NMR studies. Here, we report the assignment of the subunit F.
Shovanlal Gayen and Subramanian Vivekanandan contributed equally to this work. 相似文献