• Molecules and Cells
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• v.22 no.1
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• pp.13-20
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• 2006

Hepatitis C virus (HCV) non-structural protein 5A protein (NS5A), which consists of three functional domains, is involved in regulating viral replication, interferon resistance, and apoptosis. Recently, the three-dimensional structure of the domain 1 was determined. However, currently the molecular basis for the domains 2 and 3 of HCV NS5A is yet to be defined. Toward this end, we expressed, purified the domain 2 of the NS5A (NS5A-D2), and then performed biochemical and structural studies. The purified domain 2 was active and was able to bind NS5B and PKR, biological partners of NS5A. The results from gel filtration, CD analysis, 1D $^1H$ NMR and 2D $^1H-^{15}N$ heteronuclear single quantum correlation (HSQC) spectroscopy indicate that the domain 2 of NS5A appears to be flexible and disordered.

• IMMUNE NETWORK
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• v.2 no.3
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• pp.137-141
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• 2002

Among the members of the inhibitor of apoptosis (IAP) protein family, only Livin and survivin have been reported to have variant forms. We have found a variant form of c-IAP2 through the interaction with the X protein of HBV using the yeast two-hybrid system. In contrast to the wild-type c-IAP2, the variant form has two stretches of sequence in the RING domain that are repeated in the C-terminus that would disrupt the RING domain. We demonstrate that the variant form has an inhibitory effect on TNF-mediated $NF-{\kappa}B$ activation unlike the wild-type c-IAP2, which increases TNFmediated $NF-{\kappa}B$ activation. These results suggest that this variant form has different activities from the wild-type and the RING domain may be involved in the regulation of TNF-induced $NF-{\kappa}B$ activation.

• Development and Reproduction
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• v.17 no.4
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• pp.299-309
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• 2013

Transforming growth factor (TGF) family is well known to induce the chondrogenic differentiation of mesenchymal stem cells (MSC). However, the precise signal transduction pathways and underlying factors are not well known. Thus the present study aims to evaluate the possible role of C2 domain in the chondrogenic differentiation of human mesenchymal stem cells. To this end, 145 C2 domains in the adenovirus were individually transfected to hMSC, and morphological changes were examined. Among 145 C2 domains, C2 domain of protein kinase C eta ($PKC{\eta}$) was selected as a possible chondrogenic differentiation factor for hMSC. To confirm this possibility, we treated $TGF{\beta}3$, a well known chondrogenic differentiation factor of hMSC, and examined the increased-expression of glycosaminoglycan (GAG), collagen type II (COL II) as well as $PKC{\eta}$ using PT-PCR, immunocytochemistry and Western blot analysis. To further evaluation of C2 domain of $PKC{\eta}$, we examined morphological changes, expressions of GAG and COL II after transfection of $PKC{\eta}$-C2 domain in hMSC. Overexpression of $PKC{\eta}$-C2 domain induced morphological change and increased GAG and COL II expressions. The present results demonstrate that $PKC{\eta}$ involves in the TGF-${\beta}3$-induced chondrogenic differentiation of hMSC, and C2 domain of $PKC{\eta}$ has important role in this process.

• The Korean Journal of Ceramics
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• v.7 no.1
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• pp.30-35
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• 2001

The contribution of the non-$180^{\circ}C$ domains to the electric-field-induced strains (EFI-strains) of PZT ceramics was evaluated by an XRD method and by an interferometric method. The XRD intensity ratio of 200 and 002 diffraction peaks of tetragonal PZT was measured under strong electric fields. The amount of the $90^{\circ}$ domain reorientation was evaluated and the strain due to the domain reorientation was calculated. It was confirmed that the EFI-strain of PZT ceramics was equal to the sum of the strain calculated from the d$_33$ constant determined by the resonance-antiresonance method and the strain due to the $90^{\circ}$ domain reorientation. The amount of the $90^{\circ}$domain reorientation has a linear relation with the c/a ratio in the "soft" PZT ceramics. A Mech-Zehnder interferometer was constructed to measure the EFI-strains vs. electric-field curves of PZT ceramics as a function of frequency. The EFI-strain vs. electric-field curve showed a hysteresis due to the effect of the non-$180^{\circ}$ domain reorientation when the applied voltage was high and its frequency was low. The apparent piezoelectric constant increased from the d$_33$ value determined by the resonance-antiresonance method with decreasing frequency. This deviation was attributed to the non-$180^{\circ}$ domain contribution.tribution.

• Journal of the Korean Magnetic Resonance Society
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• v.20 no.2
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• pp.50-55
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• 2016

Backbone $^1H$, $^{13}C$ and $^{15}N$ resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot-Marie-Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [$^{13}C/^{15}N$]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.

• Molecules and Cells
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• v.44 no.3
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• pp.179-185
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• 2021

Vancomycin response regulator (VncR) is a pneumococcal response regulator of the VncRS two-component signal transduction system (TCS) of Streptococcus pneumoniae. VncRS regulates bacterial autolysis and vancomycin resistance. VncR contains two different functional domains, the N-terminal receiver domain and C-terminal effector domain. Here, we investigated VncR C-terminal DNA binding domain (VncRc) structure using a crystallization approach. Crystallization was performed using the micro-batch method. The crystals diffracted to a 1.964 Å resolution and belonged to space group P212121. The crystal unit-cell parameters were a = 25.71 Å, b = 52.97 Å, and c = 60.61 Å. The structure of VncRc had a helix-turn-helix motif highly similar to the response regulator PhoB of Escherichia coli. In isothermal titration calorimetry and size exclusion chromatography results, VncR formed a complex with VncS, a sensor histidine kinase of pneumococcal TCS. Determination of VncR structure will provide insight into the mechanism by how VncR binds to target genes.

• Transactions of Materials Processing
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• v.22 no.5
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• pp.258-263
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• 2013

The deformation behavior of NIMONIC 80A was studied in the high temperature range of $900{\sim}1200^{\circ}C$ and for strain rates varying between 0.02 and $20s^{-1}$ via the hot compression test. Processing maps for hot working were constructed on the basis of the power dissipation efficiency using a dynamic material model. The results showed that the strength during hot compression increased with increasing strain rate and decreasing temperature. At low strains, the processing map of NIMONIC 80A did not reveal any instability domain regardless of the strain rate and temperature. However, at high strains, the processing map exhibited an instability domain at a low strain rate of $0.2s^{-1}$ and within a temperature range of $900{\sim}960^{\circ}C$. In the instability domain, the deformed microstructure exhibited shear bands and carbide precipitation while, in the safe domain, full recrystallization occurred.

• Proceedings of the Korean Society of Food Hygiene and Safety Conference
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• 2002.05a
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• pp.215-215
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• 2002

Catalytic subunit of pyruvate dehydrogenase phosphatase (PDPc) has been suggested to have three major funational domains such as dihydrplipoamide adetyltransferase(E2)-binding domain, regulatory subunit of PDP(PDP)r-binding domain, and calcium-binding domain. In order to identify functional domains, recombinant catalytic subunit of pyruvate dehydrogenase phosphatase(rPDPc) was expressed in E. coli JM101 and purified to near homogeneity using the unique property of PDPc: PDPc binds to the inner lipoyl domain (L2) of E2 of ppyruvate dehydrogenase complex (PDC) in the presence of Ca+2, not under EGTA. PDPc was limited-proteolysed by typsin, chymotypsin, Arg-C, and elastase at pH 7.0 and 30C and N-terminal analysis of the fragments was done. Chymotrypsin, trypsin, and elastase made two major fragments: N-terminal large fragment, approx. 50kD and C-terminal small fragment, approx.10 kDa. Arg-C made three major fragments: N-terminal fragment, approx. 35kD, and central fragment, approx. 15 kD, and C-terminal fragment, approx. 10 kD. This study strongly suggest that PDPc consists of three major functional domains. However, further study should be necessary to identify the functional role.

• Korean Journal of Biological Psychiatry
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• v.20 no.3
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• pp.63-65
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• 2013

The new edition of the Diagnostic and Statistical Manual of Mental Disorders (DSM-5) is published by the American Psychiatric Association. The diagnostic systems for mental disorders have come under criticism for relying on presenting signs and symptoms with the result that they do not adequately reflect relevant neurobiological and behavioral systems. Finally, the National Institute of Mental Health (NIMH) in the United States has suggested the Research Domain Criteria (RDoC) to develop a research classification system based upon dimensions of neurobiology and behavioral aspect. The present review introduces the RDoC as a new reaseach framework.

• Journal of the Korean Mathematical Society
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• v.49 no.1
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• pp.17-30
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• 2012

Let D be an arbitrary domain in $\mathbb{C}^n$, n > 1, and $M{\subset}{\partial}D$ be an open piece of the boundary. Suppose that M is connected and ${\partial}D$ is smooth real-analytic of finite type (in the sense of D'Angelo) in a neighborhood of $\bar{M}$. Let f : $D{\rightarrow}\mathbb{C}^n$ be a holomorphic correspondence such that the cluster set $cl_f$(M) is contained in a smooth closed real-algebraic hypersurface M' in $\mathbb{C}^n$ of finite type. It is shown that if f extends continuously to some open peace of M, then f extends as a holomorphic correspondence across M. As an application, we prove that any proper holomorphic correspondence from a bounded domain D in $\mathbb{C}^n$ with smooth real-analytic boundary onto a bounded domain D' in $\mathbb{C}^n$ with smooth real-algebraic boundary extends as a holomorphic correspondence to a neighborhood of $\bar{D}$.