• 생명과학회지
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• 제14권5호
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• pp.732-740
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• 2004

MCM 단백질의 암세포내에서 과발현 되는 원인을 규명하기 위하여 mcm7, 2 promoter영역의 전사인자 결합 부위의 역할을 조사하였다. 암세포에서 promoter 활성은 정상세포보다 8배정도 높은 활성을 나타내 특유 전사인자의 존재를 시사하였다. Promoter영 역 에는 E2F 결합부위 와 Myc/Max/Mad단백질 결합 부위로 알려진 I-box가 존재한다. 이들 각각의 변이체 promoter를 작성하여 암세포와 정상세포에서 luciferase reporter 활성을 측정하는 것으로 각 영역의 역할을 검토하였다. 그 결과 정상세포 내에서는 강한 repressor존재 또는 활성을 negative로 조절 할 수 있는 complex의 존재로 promoter활성이 조절되는 반면 암세포 내에서는 I-box에 결합하여 promoter를 활성화시키는 특유 단백질의 존재가 시사되었다.

• Animal cells and systems
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• 제7권4호
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• pp.337-343
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• 2003

Methyl jasmonate (MeJA) is a signal molecule in the activation of defense responses in plants. In this study, we isolated 15 MeJA-inducible genes by subtractive hybridization. These genes encode two myrosinase-binding proteins, five lipase-like proteins, a polygalacturonase inhibitor, a putative chlorophyll-associated protein, a terpene synthase, a dehydroascorbate reductase, an ascorbate oxidase, a cysteine protease, an O-methyltransferase, and an epithiospecifier protein. Northern analysis showed that most of the Chinese cabbage genes are barely expressed in healthy leaves, but are strongly induced by MeJA treatment. We also examined whether these MeJA-inducible genes were activated by ethethon, BTH, and Pseudomonas syringae pv. tomato (Pst), a nonhost pathogen of Chinese cabbage. The results showed that none of the MeJA-inducible genes was strongly induced by ethephon or by BTH. The genes encoding lipase-like proteins and a myrosinase-binding protein were weakly induced by Pst. Other MeJA-inducible genes were not activated at all by the pathogen.

• BMB Reports
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• 제34권2호
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• pp.95-101
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• 2001

Tissue transglutaminase (TGII, $G{\alpha}h$) belongs to a family of enzymes which catalyze post-translational modification of proteins by forming isopeptides via $Ca^{2+}$-dependent reaction. Although TGII-mediated formation of isopeptides has been implicated to play a role in a variety of cellular processes, the physiological function of TGII remains unclear. In addition to this Tease activity, TGII is a guanosine triphosphatase (GTPase) which binds and hydrolyzes GTP It is now well recognized that the GTPase action of TGII regulates a receptor-mediated transmembrane signaling, functioning as a signal transducer of the receptor. This TGII function signifies that TGII is a new class of GTP-binding regulatory protein (G-protein) that differs from "Classical" heterotrimeric G-proteins. Regulation of enzyme is an important biological process for maintaining cell integrity. This review summarizes the recent development in regulation of TGII that may help for the better understanding of this unique enzyme. Since activation and inactivation of GTPase of TGII are similar to the heterotrimeric G-proteins, the regulation of heterotrimeric G-protein in the transmembrane signaling is also discussed.

• Journal of Industrial and Engineering Chemistry
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• 제67권
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• pp.293-300
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• 2018

Lipocalins are diverse group of small extracellular proteins found in various organisms. In this study, members of 10 non-homologous lipocalin-ligand crystal complex structures were remodeled using rigid and flexible ligand modes to validate the prediction efficiency of molecular docking simulation. The modeled ligand conformations indicated a high prediction accuracy in rigid ligand mode using cluster based analysis for most cases whereas the flexible ligand mode required further considerations such as ligand binding energy and RMSD for some cases. This in silico study is expected to serve as a platform in the screening of novel ligands against lipocalin family of proteins.

• 한국미생물학회:학술대회논문집
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• 한국미생물학회 2002년도 추계학술대회
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• pp.159-161
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• 2002

Bacteriophage lambda integrase carries out the site-specific recombination of lambda. Integrase contains two DNA binding domains with distinct sequence specificity, namely arm-type binding and core-type binding domains. The amino-terminal arm-binding domain is structurally related to the three-stranded $\beta-sheet$ family of DNA-binding domains. Integrase binding to the high affinity arm-type site by the amino-terminal domain facilitates Int binding to the low affinity core-type site, where the cleavage and strand exchange occurs. The amino-terminal domain of Int also modulates the core-binding and catalysis through intramolecular domain-domain interaction and/or intermolecular interactions between Int monomers. In addition, the amino-terminal domain interacts cooperatively with excisionase during excision. This indicates that amino-terminal domain of Int plays an important role in formation of proper higher-order nucleoprotein structure required for lambda site-specific recombination.

• 한국동물위생학회지
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• 제44권4호
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• pp.185-194
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• 2021

Polyglutamine extension in the coding sequence of mutant huntingtin causes neuronal degeneration associated with the formation of insoluble polyglutamine aggregates in Huntington's disease (HD). Mutant huntingtin can form aggregates within the nucleus and processes of neurons possibly due to misfolding of the proteins. To better understand the mechanism by which an elongated polyglutamine causes aggregates, we have developed an in vitro binding assay system of polyglutamine tract from truncated huntingtin. We made GST-HD exon1 fusion proteins which have expanded polyglutamine epitopes (e.g., 17, 23, 32, 46, 60, 78, 81, and 94 CAG repeats). In the present emergence of new study adjusted nanotechnology on protein chip such as surface plasmon resonance strategy which used to determine the substance which protein binds in drug discovery platform is worth to understand better neurodegenerative diseases (i.e., Alzheimer disease, Parkinson disease and Huntington disease) and its pathogenesis along with development of therapeutic measures. Hence, we used strengths of surface plasmon resonance (SPR) technology which is enabled to examine binding specificity and explore targeted molecular epitope using its electron charged wave pattern in HD pathogenesis utilize conjugated mutant epitope of HD protein and its interaction whether wild type GST-HD interacts with mutant GST-HD with maximum binding affinity at pH 6.85. We found that the maximum binding affinity of GST-HD17 with GST-HD81 was higher than the binding affinities of GST-HD17 with other mutant GST-HD constructs. Furthermore, our finding illustrated that the mutant form of GST-HD60 showed a stronger binding to GST-HD23 or GST-HD17 than GST-HD60 or GST-HD81. These results indicate that the binding affinity of mutant huntingtin does not correlate with the length of polyglutamine. It suggests that the aggregation of an expanded polyglutamine might have easily occurred in the presence of wild type form of huntingtin.

• 대한화학회지
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• 제68권3호
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• pp.151-159
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• 2024

Indian spices are well known for their numerous health benefits, flavour, taste, and colour. Recent Advancements in chemical technology have led to better extraction and identification of bioactive molecules (phytochemicals) from spices. The therapeutic effects of spices against diabetes, cardiac problems, and various cancers has been well established. The present in silico study aims to investigate the binding affinity of 29 phytochemicals from 11 Indian spices with two prominent proteins, BCL3 and CXCL10 involved in invasiveness and bone metastasis of breast cancer. The three-dimensional structures of 29 phytochemicals were extracted from PubChem database. Protein Data Bank was used to retrieve the 3D structures of BCL3 and CXCL10 proteins. The drug-likeness and other properties of compounds were analysed by ADME and Lipinski rule of five (RO5). All computational simulations were carried out using Autodock 4.0 on Windows platform. The proteins were set to be rigid and compounds were kept free to rotate. In-silico study demonstrated a strong complex formation (positive binding constants and negative binding energy ΔG) between all phytochemicals and target proteins. However, piperine and sesamolin demonstrated high binding constants with BCL3 (50.681 × 10³ mol^-1, 137.76 × 10³ mol^-1) and CXCL10 (98.71 × 10³ mol^-1, 861.7 × 10³ mol^-1), respectively. The potential of these two phytochemicals as a drug candidate was highlighted by their binding energy of -6.5 kcal mol^-1, -7.1 kcal mol^-1 with BCL3 and -6.9 kcal mol^-1, -8.2 kcal mol^-1 with CXCL10, respectively coupled with their favourable drug likeliness and pharmacokinetics properties. These findings underscore the potential of piperine and sesamolin as drug candidates for inhibiting invasiveness and regulating breast cancer metastasis. However, further validation through in vitro and in vivo studies is necessary to confirm the in silico results and evaluate their clinical potential.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1998년도 학술발표회
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• pp.11-11
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• 1998

Zinc fingers of Cys$_2$His$_2$ class constitute one of the most common DNA binding motifs in eukaryotes. Unlike other DNA binding motifs, zinc finger proteins recognize very diverse DNA sites, and their sequence specificities can be systematically changed by phage display.(omitted)

• 한국동물학회:학술대회논문집
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• 한국동물학회 2003년도 한국생물과학협회 학술발표대회
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• pp.190.4-190
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• 2003

No Abstract, See Full Text

• 생명과학회지
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• 제27권10호
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• pp.1191-1198
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• 2017

세포 내 소기관들과 소포들은 세포 내에서 미세소관을 따라 적절한 구획으로 수송된다. 이러한 세포 내 수송과정은 분자 모터단백질인 kinesin과 dynein에 의하여 이루어진다. Kinesin 1은 오징어 축삭돌기 세포질로부터 처음 분리되었으며 2개의 중쇄단위체(KHCs, 또는 KIF5s) 및 이와 결합하는 경쇄단위체(KLCs)의 복합체를 형성한다. KIF5s는C-말단 고리 영역을 통해 많은 다양한 단백질과 결합하는데, 아직 그 결합단백질들은 충분히 밝혀지지 않았다. 본 연구에서는 KIF5A 결합단백질을 분리하기 위하여 효모 two-hybrid 탐색을 수행하여 스트레스 과립형성과 mRNP 위치결정에 관여하는 Ras-GTPase-activating protein (GAP) Src homology3 (SH3)-domain-binding protein 2 (G3BP2)를 분리하였다. G3BP2는 KIF5A의 C-말단 고리 영역에 존재하는 73개 아미노산을 포함하는 영역과 결합하였다. 그러나 G3BP2는 KIF5B, KIF5C, KLC1, KIF3A와는 결합하지 않았다. KIF5A는 G3BP2의 arginine-glycine-glycine(RGG)/Gly-rich 도메인과 결합하지만 G3BP1과는 결합하지 않았다. HEK-293T세포에 G3BP2와 KIF5A를 발현하여 면역침강한 결과 G3BP2와 KIF5A는 같이 침강하였다. 또한 HEK-293T 세포 내의 전체에서 두 단백질은 같은 부위에 존재하였다. 이러한 결과들은 세포 내에서 G3BP2는 KIF5A와 결합하는 결합단백질로 확인 되었다.