• 제목/요약/키워드: Molecular interaction

검색결과 1,519건 처리시간 0.036초

Interaction of Naegleria fowleri Trophozoites with Escherichia coli and MRSA by N-acetylglucosamine and Galactose

  • Son, Dae-Hyun;Jung, Suk-Yul
    • 대한의생명과학회지
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    • 제27권4호
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    • pp.323-328
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    • 2021
  • Naegleria fowleri is a free-living amoeba causing primary amoebic encephalitis. In this study, we analyzed how the N-aceytlglucosamine (GlcNAc) and D-galactose affected the interaction between Naegleria fowleri and methicillin-resistant Staphylococcus aureus (MRSA) or Escherichia coli O157:H7, and the interaction with bacteria when monosaccharides were treated with N. fowleri for a longer pre-incubation time. When GlcNAc was treated with N. fowleri for 1 hr, the E. coli association was almost the same as that of the control not treated with GlcNAc until the concentration of GlcNAc was 25 mM. However, the E. coli association was reduced by approximately 91% with 100 mM GlcNAc. E. coli invasion into N. fowleri showed statistical significance only in the group treated with 100 mM GlcNAc. The interaction when treated with galactose showed a very different pattern in the 50 mM galactose group than when treated with GlcNAc. In the MRSA interaction, a statistically significant decrease in association (76.3% by GlcNAc and 88.7% by galactose) and invasion (3.6% by GlcNAc and 9.3% by galactose) was shown by the concentration of two 100 mM monosaccharides. The group treated with monosaccharides at the same time showed almost no difference in all interactions from the group treated with monosaccharides at the same time. Taken together, it suggested that the effect of monosaccharides on the interaction of several Gram-negative or positive bacteria and the evidence that the interaction could be enhanced by longer pre-incubation time.

공유결합과 친화력결합에 의한 고정화 Trypsin의 효소역가와 절단특성 비교 (Comparison of Enzymatic Activity and Cleavage Characteristics of Trypsin Immobilized by Covalent Conjugation and Affinity Interaction)

  • 장대호;성기훈;이은규
    • KSBB Journal
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    • 제21권4호
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    • pp.279-285
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    • 2006
  • 본 연구에서는 trypsin을 모델 단백질로 하여 단백질 본연의 환성을 유지할 수 있는 고정화 방법을 찾기 위하여 공유결합방법과 친화력 결합방법을 이용하여 trypsin을 고정화 하였다. Streptavidin-biotin system을 이용한 고정화 방법은 bioactivity 유지측면에서 공유결합 방법보다 우수함을 확인하였다. 하지만 streptavidin-biotin system을 이용하였을 때 고정화 수율이 낮은 것은 해결해야 할 과제이다. 분자량이 다른 기질들(BAPNA, insulin, BSA)을 대상으로 고정화 trypsin의 부위 특이적 절단 특성을 분석한 결과 streptavidin-biotin에 의해 고정화된 trypsin이 절단효율도 높고 sequence coverage도 높은 것으로 확인되었다. 또한 공유결합된 trypsin은 견고한 분자구조를 나타낸 반면 streptavidin-biotin system으로 고정화된 trypsin은 유연성이 높은 것을 QCM-D를 이용하여 관찰할 수 있었다. 따라서 streptavidin-biotin system에 의한 고정화 방법에서 streptavidin-biotin 결합이 일종의 spacer arm 역할을 하면서 고정화된 trypsin의 분자유연성을 향상시켜 절단반응의 부위특이성과 절단수율을 향상시키는 것으로 판단되었다.

Aspergillus nidulans 분비소낭 구성요소인 α-COP과 ε-COP의 결합 부위 분석 (Analysis of Protein Domain for Interaction between α-COP and ε-COP in Aspergillus nidulans)

  • 송은정;김기현;이환희;박정석;강은혜;박희문
    • 한국균학회지
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    • 제40권4호
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    • pp.224-228
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    • 2012
  • A. nidulans ${\alpha}$-COP과 상호작용하는 단백질을 동정하기 위하여 ${\alpha}$-COP을 암호하는 유전자를 bait로 yeast two-hybrid 스크리닝용 A. nidulans cDNA 라이브러리를 탐색한 결과, COPI 소낭의 구성요소 중 하나인 ${\varepsilon}$-COP을 암호화하고 있는 유전자를 동정하고 $aneA^+$($\underline{A}$spergillus $\underline{n}$idulans $\underline{e}$psilon-COP, $AN{\varepsilon}$-COP)으로 명명하였다. $aneA^+$ 유전자는 총 296개의 아미노산을 암호화하고 있으며, 다른 균류의 ${\varepsilon}$-COP과 높은 상동성을 보였다. Yeast two hybrid 시스템으로 두 단백질 간의 상호작용 부위를 분석한 결과, ${\alpha}$-COP의 COOH 도메인과 ${\varepsilon}$-COP의 C-말단부가 필수 부위였으며, ${\alpha}$-COP N-말단의 WD 도메인과 ${\varepsilon}$-COP의 TPR 부위는 두 단백질 간의 결합을 촉진하는 조절부위로 밝혀졌다. 또한 사상균인 A. nidulans와 효모류인 S. cerevisiae에서 ${\alpha}$-COP과 ${\varepsilon}$-COP 간 작용양상이 유사한 것으로 보아, COPI 소낭의 구성요소인 ${\alpha}$-COP과 ${\varepsilon}$-COP 간의 상호작용 기전은 진핵세포 내에서 진화적으로 잘 보존되어 있는 것으로 추정되었다.

Molecular interaction of $G{\alpha}16$ subunit G protein with chemoattractant receptors

  • Ha, Ji-Hee;Lee, Chang-Ho
    • 대한약학회:학술대회논문집
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    • 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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    • pp.275.1-275.1
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    • 2002
  • It has been proposed that G protein interacts with receptor via multiple interaction sites. With regard to this, C-terminus of the G${\alpha}$ subunit is clearly not the only structural determinant on the G proteins that is critical for receptor coupling selectivity, but the extreme N-terminus of Ga subunit and other structural elements were proposed to be responsible for dictating the interaction with receptors. (omitted)

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Molecular Vibration-Activity Relationship in the Agonism of Adenosine Receptors

  • Chee, Hyun Keun;Oh, S. June
    • Genomics & Informatics
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    • 제11권4호
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    • pp.282-288
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    • 2013
  • The molecular vibration-activity relationship in the receptor-ligand interaction of adenosine receptors was investigated by structure similarity, molecular vibration, and hierarchical clustering in a dataset of 46 ligands of adenosine receptors. The resulting dendrogram was compared with those of another kind of fingerprint or descriptor. The dendrogram result produced by corralled intensity of molecular vibrational frequency outperformed four other analyses in the current study of adenosine receptor agonism and antagonism. The tree that was produced by clustering analysis of molecular vibration patterns showed its potential for the functional classification of adenosine receptor ligands.

Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF)

  • Park, Young-Hoon;Jeong, Mi Suk;Jang, Se Bok
    • BMB Reports
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    • 제49권3호
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    • pp.159-166
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    • 2016
  • Several members of tumor necrosis factor receptor (TNFR) superfamily that these members activate caspase-8 from death-inducing signaling complex (DISC) in TNF ligand-receptor signal transduction have been identified. In the extrinsic pathway, apoptotic signal transduction is induced in death domain (DD) superfamily; it consists of a hexahelical bundle that contains 80 amino acids. The DD superfamily includes about 100 members that belong to four subfamilies: death domain (DD), caspase recruitment domain (CARD), pyrin domain (PYD), and death effector domain (DED). This superfamily contains key building blocks: with these blocks, multimeric complexes are formed through homotypic interactions. Furthermore, each DD-binding event occurs exclusively. The DD superfamily regulates the balance between death and survival of cells. In this study, the structures, functions, and unique features of DD superfamily members are compared with their complexes. By elucidating structural insights of DD superfamily members, we investigate the interaction mechanisms of DD domains; these domains are involved in TNF ligand-receptor signaling. These DD superfamily members play a pivotal role in the development of more specific treatments of cancer.

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.

Identification of the Interaction between Rat Translationally Controlled Tumor Protein/IgE-dependent Histamine Releasing Factor and Myosin Light Chain

  • Kim, Min-Jeong;Jung, Jae-Hoon;Choi, Eung-Chil;Park, Hae-Young;Lee, Kyung-Lim
    • BMB Reports
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    • 제34권6호
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    • pp.526-530
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    • 2001
  • The translationally controlled tumor protein (TCTP), also known as the IgE-dependent histamine releasing factor (HRF), was used in the yeast two-hybrid system to screen the interacting molecules. We obtained the N-terminus truncated rat fast myosin alkai light chain from the rat skeletal muscle cDNA library in the screening. Since either TCTP/HRF or the myosin light chain is known to be associated with histamine secretion from RBL-2H3 cells, we investigated the possible interaction between rat TCTP/HRF and nonmuscle myosin light chain in these cells. We used affinity chromatography and coimmunoprecipitation. Our data suggests that HRF and the myosin light chain interact, which may play an important role in histamine release in RBL-2H3 cells.

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GRP94는 thyroglobulin의 folding에 관여한다. (Overexpression of ER Resident Molecular Chaperones and Characterization of Their Interaction with Thyroglobulin in FRTL5 cells.)

  • Seong, Yeon-Mun;Shong, MinHo;Kwon, O-Yu
    • 생명과학회지
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    • 제9권1호
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    • pp.76-83
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    • 1999
  • Endoplasmic reticulum (ER)내에 단백질의 folding과 안정화에 관여하는 단백질을 molecular cha-perone이라고 한다. GRP94 역시 ER내에 존재하는 molecular chaperone으로 알려지고 있지만 갑상선세포에서 단백질의 folding에 관여한다는 증거는 아직 불충분하다. 본 설험은 molecular chaperone을 세포내에서 overexpression시킬 수 있는 system을 확립하였다. 그 중에서 GRP94가 단백질의 folding에 직접적으로 관여한다는 증거를 얻기 위하여, endogenous GRP94를 code한 cDNA를 overexpression vector에 의해서 forced expression시킴으로 신생thyroglobulin의 folding에 직접적으로 관여하는 증거를 immun-oprecipitation으로 증명하였다.

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