• 제목/요약/키워드: structural biology

검색결과 847건 처리시간 0.025초

Structural and Functional Insight into Proliferating Cell Nuclear Antigen

  • Park, So Young;Jeong, Mi Suk;Han, Chang Woo;Yu, Hak Sun;Jang, Se Bok
    • Journal of Microbiology and Biotechnology
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    • 제26권4호
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    • pp.637-647
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    • 2016
  • Proliferating cell nuclear antigen (PCNA) is a critical eukaryotic replication accessory factor that supports DNA binding in DNA processing, such as DNA replication, repair, and recombination. PCNA consists of three toroidal-shaped monomers that encircle double-stranded DNA. The diverse functions of PCNA may be regulated by its interactions with partner proteins. Many of the PCNA partner proteins generally have a conserved PCNA-interacting peptide (PIP) motif, located at the N- or C- terminal region. The PIP motif forms a 310 helix that enters into the hydrophobic groove produced by an interdomain-connecting loop, a central loop, and a C-terminal tail in the PCNA. Post-translational modification of PCNA also plays a critical role in regulation of its function and binding partner proteins. Structural and biochemical studies of PCNA-protein will be useful in designing therapeutic agents, as well as estimating the outcome of anticancer drug development. This review summarizes the characterization of eukaryotic PCNA in relation to the protein structures, functions, and modifications, and interaction with proteins.

Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar

  • Kim, Dong-Uk;Yoo, Ji-Ho;Lee, Yong-Joo;Kim, Kwan-Soo;Cho, Hyun-Soo
    • BMB Reports
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    • 제41권1호
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    • pp.48-54
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    • 2008
  • PM0188 is a newly identified sialyltransferase from P. multocida which transfers sialic acid from cytidine 5'-monophosphonuraminic acid (CMP-NeuAc) to an acceptor sugar. Although sialyltransferases are involved in important biological functions like cell-cell recognition, cell differentiation and receptor-ligand interactions, little is known about their catalytic mechanism. Here, we report the X-ray crystal structures of PM0188 in the presence of an acceptor sugar and a donor sugar analogue, revealing the precise mechanism of sialic acid transfer. Site-directed mutagenesis, kinetic assays, and structural analysis show that Asp141, His311, Glu338, Ser355 and Ser356 are important catalytic residues; Asp141 is especially crucial as it acts as a general base. These complex structures provide insights into the mechanism of sialyltransferases and the structure-based design of specific inhibitors.

On the genus Rhodella, the emended orders Dixoniellales and Rhodellales with a new order Glaucosphaerales (Rhodellophyceae, Rhodophyta)

  • Scott, Joe;Yang, Eun-Chan;West, John A.;Yokoyama, Akiko;Kim, Hee-Jeong;De Goer, Susan Loiseaux;O'Kelly, Charles J.;Orlova, Evguenia;Kim, Su-Yeon;Park, Jeong-Kwang;Yoon, Hwan-Su
    • ALGAE
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    • 제26권4호
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    • pp.277-288
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    • 2011
  • The marine unicellular red algal genus Rhodella was established in 1970 by L. V. Evans with a single species R. maculata based on nuclear projections into the pyrenoid. Porphyridium violaceum was described by P. Kornmann in 1965 and transferred to Rhodella by W. Wehrmeyer in 1971 based on plastid features and the non-parietal position of the nucleus. Molecular and fine structural evidences have now revealed that Rhodella maculata and R. violacea are one species, so R. violacea has nomenclatural priority and the correct name is Rhodella violacea (Kornmann) Wehrmeyer. The status of families within Rhodellophyceae was examined. The order Dixoniellales and family Dixoniellaceae are emended to include only Dixoniella and Neorhodella. The order Rhodellales and family Rhodellaceae are emended to include Rhodella and Corynoplastis. Glaucosphaera vacuolata Korshikov and the Glaucosphaeraceae Skuja (1954) with an emended description are transferred to the Glaucosphaerales ord. nov.

Overexpression and Biological Characterization of the Death Domain Complex between TRADD and FADD

  • Hwang, Eun Young;Jeong, Mi Suk;Sung, Minkyung;Jang, Se Bok
    • Bulletin of the Korean Chemical Society
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    • 제34권4호
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    • pp.1089-1095
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    • 2013
  • The tumor necrosis factor-receptor 1 (TNFR1)-associated death domain protein (TRADD) contains an N-terminal TRAF binding domain and a C-terminal death domain. TRADD is known to interact directly with TNF receptor 2 (TNFR2) and the Fas-associated death domain protein (FADD), which are signal transducers that activate NF-${\kappa}B$ and induce apoptosis, respectively. To date, there has been no structural information on the TRADD and FADD death domain (DDs) complex. In this study, the death domains of TRADD and FADD were co-expressed and purified from Escherichia coli for structural characterization. We found that human TRADD (hTRADD) interacted strongly with mouse FADD (mFADD) via their DDs and interacted weakly with human FADD (hFADD)-DD. Moreover, the structures of the TRADD-DD:FADD-DD complexes were separately modeled from predicted structures in the protein data bank (PDB). The results of this study will have important applications in human diseases such as cancer, AIDS, degenerative and autoimmune diseases, and infectious diseases.

Structural Study of Monomethyl Fumarate-Bound Human GAPDH

  • Park, Jun Bae;Park, Hayeong;Son, Jimin;Ha, Sang-Jun;Cho, Hyun-Soo
    • Molecules and Cells
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    • 제42권8호
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    • pp.597-603
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    • 2019
  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a core enzyme of the aerobic glycolytic pathway with versatile functions and is associated with cancer development. Recently, Kornberg et al. published the detailed correlation between GAPDH and di- or monomethyl fumarate (DMF or MMF), which are well-known GAPDH antagonists in the immune system. As an extension, herein, we report the crystal structure of MMF-bound human GAPDH at $2.29{\AA}$. The MMF molecule is covalently linked to the catalytic Cys152 of human GAPDH, and inhibits the catalytic activity of the residue and dramatically reduces the enzymatic activity of GAPDH. Structural comparisons between $NAD^+$-bound GAPDH and MMF-bound GAPDH revealed that the covalently linked MMF can block the binding of the $NAD^+$ cosubstrate due to steric hindrance of the nicotinamide portion of the $NAD^+$ molecule, illuminating the specific mechanism by which MMF inhibits GAPDH. Our data provide insights into GAPDH antagonist development for GAPDH-mediated disease treatment.

赤裳山의 植生 (The Vegetation of Mt. Choksang)

  • Kim, Chang-Hwan;Seon-Hee Kang;Bong-Seop Kil
    • The Korean Journal of Ecology
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    • 제14권2호
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    • pp.137-148
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    • 1991
  • The forest vegation and their structural characteristics in mt. chokang were investgated by phytosociological survey and ordination. It was classified five forests such as quercus tschonoskii community and fraxinus mandshurica community and this result has confirmed to coincide with community ciassification by polar ordination. Chang of diversity index was shown to decase, whereas dominance index, to increase according to chang high altitude. By soil moisture gradient, distribution pattern of fraxinus mandshurica, acer mono, carpinus cordata was in moist, but quercus serrata,˘quercus variabilis and mongolica, dry habitats.

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Structural Changes of the Spinach Photosystem II Reaction Center After Inactivation by Heat Treatment

  • Jang, Won-Cheoul;Tae, Gun-Sik
    • BMB Reports
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    • 제29권1호
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    • pp.58-62
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    • 1996
  • The structural changes in the electron donor side of the PSII reaction center have been monitored since heat treatment ($45^{\circ}C$ for 5 min) of thylakoids is known to decrease the oxygen evolving activity. In heat-treated spinach chloroplast thylakoids, the inhibitory effect of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) on the electron transport activity of the PSII reaction center from diphenyl carbazide to dichlorophenolindophenol became reduced approximately 3.8 times and [$^{14}C$]-labeled DCMU binding on the D1 polypeptide decreased to 25~30% that of intact thylakoid membranes, implying that the conformational changes of the DCMU binding pocket, residing on the D1 polypeptide, occur by heat treatment. The accessibility of trypsin to the $NH_2$-terminus of the cytochrome b-559 ${\alpha}$-subunit, assayed with Western blot using an antibody generated against the synthetic peptide (Arg-68 to Arg-80) of the COOH-terminal domain, was also increased, indicating that heat-treatment caused changes in the structural environments near the stromal side of the cytochrome b-559 ${\alpha}$-subunit, allowing trypsin more easily to cleave the $NH_2$-terminal domain. Therefore, the structural changes in the electron donor side of the PSII reaction center complexes could be one of the reasons why the oxygen evolving activity of the heat-treated thylakoid membranes decreased.

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Structural Changes on the HL-60 Cells of TPA-induced Adherence by Asadisulphide

  • Ahn, Byung-Zun;Kim, Seon-Hee;Park, Mi-A;You, Kwan-Hee
    • 대한의생명과학회지
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    • 제8권1호
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    • pp.13-20
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    • 2002
  • Asadisulphide were purified from Ferrula assafoetida by organic solvent extraction and chromatography. Since ethyl acetate extracts of F. assafoetida has the strongest inhibitory effects on adherence of HL-60 cells, it was reextracted with ethyl acetate, hexane, and ethyl ether and chromatographed three times to isolate asadisulphide. HL-60 cells were grouped into untreated control, TPA-treated, asadisulphide-teated and TPA+asadisulphide-treated groups, and structural changes of these cells were observed using light microscope, scanning electron microscope and transmission electron microscope to examine the inhibitory effects of asadisulfide on the TPA-induced adherence of HL-60 cells. Light microscopic observations showed that asadisulphide has inhibitory effects on the cell aggregation, extention of cytoplasmic processes and inhibition of substrate adhesion of HL-60 cells. Using scanning and transmission electron microscope, it was observed that cell surfaces and several ultrastructures of TPA-treated HL-60 cell were different from control group, while there were no remarkable differences between asadisulphide-treated and TPA+asadisulphide-treated group. These results could suggest that asadisulphide has the inhibitory effects on the TPA-induced structural changes of HL-60 cells.

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