• 한국결정학회:학술대회논문집
• /
• 한국결정학회 2001년도 임시총회 및 추계학술대회연구발표회(한국결정학회)
• /
• pp.8-8
• /
• 2001

• 한국생물공학회소식지
• /
• 제18권1호
• /
• pp.80-81
• /
• 2011

• 미생물학회지
• /
• 제38권3호
• /
• pp.213-220
• /
• 2002

일본뇌염바이러스(Japanese encephalitis virus, JEV)의 구조단백질 capsid (C), precursor membrane (prM/M), 및 envelop (E) 단백질의 독립적인 발현을 위한 inducible expression system을 구축하였다. 발현세포주로는 BHK-21을 사용하였으며 발현의 induction에는 tetracycline analog인 doxycycline이 사용되었다. Transfectant BHK-21/IV(vector대조구), BHK21/IC(C), BHK-21/IP (prM/M),및 BHK-21/IE는 G418과 hygromycin 존재하에 클로닝되었으며 doxycycline induction에 따른 각 유전자의 mRNA 전사를 확인하였다. 세포의 성장곡선, chromatin condensation, internucleosomal DNA fragmentation, 및 flow cytometry에 의한 DNA content profile 분석을 통해 induction에 의한 각 구조단백질의 발현이 숙주세포에 미치는 영향을 조사하였다. 세 transfectants 모두 세포성장이 감소하고 chromatin이 응축되었다. 그러나 DNA fragmentation 및 DNA content profile 분석에서는BHK-21/IC만이 induction에 따라 상응하여 반응하였다. 이상의 결과는 JEV 감염에 의한 apoptotic 세포사멸 유도기전에서 capsid 단백질이 직접적이고 독립적인 영향요인이 될 수 있음을 제시한다.

• 한국콘텐츠학회논문지
• /
• 제8권1호
• /
• pp.259-271
• /
• 2008

본 논문에서는 단백질-단백질 상호작용과 도메인 분석을 통해 기능이 알려지지 않은 미지 단백질의 기능을 예측할 수 있는 알고리즘을 제안한다. 먼저 MIPS 데이터베이스로부터 효모에 대한 단백질-단백질 상호작용(PPI) 네트러크를 구축한다. 구축된 PPI 네트워크는(단백질 3,637개, 상호작용 10,391개) 많은 상호작용을 갖는 소수의 단백질들을 갖으면서 단백질 클러스터의 고유한 모듈성을 보이는 스케일 프리 네트워크와 계층적 네트워크의 특성을 보인다 단백질-단백질 상호작용 데이터베이스는 Y2보(Yeast Two Hybrid) 실험 등으로 얻어졌기 때문에 부정확한 데이터를 포함하고 있다. 따라서 본 논문에서는 세포상의 localization을 고려하여 부정확한 데이터를 정제하여 PPI 네트워크를 재구축한다. 그리고 허브 단백질과 네트워크 구조를 분석하여 네트워크로부터 구조적 모듈을 발견하고 이를 정의한다. 또한 이러한 구조적 모듈로부터 단백질의 도메인을 분석하여 기능적 모듈을 밝히고, 높은 확실성을 가지는 기능적 모듈을 기반으로 미지 단백질에 대한 기능을 예측한다.

• 한국결정학회:학술대회논문집
• /
• 한국결정학회 2002년도 정기총회 및 추계학술연구발표회
• /
• pp.4-4
• /
• 2002

PDZ domains bind to short segments within target proteins in a sequence-specific fashion. GRIP/ABP family proteins contain six to seven PDZ domains and interact via its sixth PDZ domain (class Ⅱ) with the C-termini of various proteins, including liprin-α. In addition the PDZ456 domain mediates the formation of homo- and heteromultimers of GRIP proteins. To better understand the structural basis of peptide recognition by a class Ⅱ PDZ domain and DZ-mediated multimerization, we determined the crystal structures of the GRIPI PDZ6 domain, alone and in complex with a synthetic C-terminal octapeptide of human liprin-α, at resolutions of 1.5 Å and 1.8 Å, respectively. Remarkably, unlike other class Ⅱ PDZ domains, Ile736 at αB5 rather than conserved Leu732 at αB1 makes a direct hydrophobic contact with the side chain of the Tyr at the -2 position of the ligand. Moreover, the peptide-bound structure of PDZ6 shows a slight reorientation of helix αB, indicating that the second hydrophobic pocket undergoes a conformational adaptation to accommodate the bulkiness of the Tyr's side chain, and forms an antiparallel dimer through an interface located at a site distal to the peptide-binding groove. This configuration may enable formation of GRIP multimers and efficient clustering of GRIP-binding proteins.

• Preventive Nutrition and Food Science
• /
• 제1권1호
• /
• pp.134-142
• /
• 1996

Diabetes carries an increased risk of atherosclerotic disease that is not fully explained by known car-diovascular risk factors. There is accumulating evidence that advanced glycation of structural proteins, and oxidation and glycation of circulating lipoproteins, are implicated in the pathogenesis of diabetic ather-osclerosis. Reactions involving glycation and oxidation of proteins and lipids are believed to contribute to atherogenesis. Glycation, the nonenzymatic binding of glucose to protein molecules, can increase the ather-ogenic potential of certain plasma constituents, including low density lipoptotein(LDL). Glycation of LDL is significant increased in diabetic patients compared with normal subjects, even in the presence of good glycemic control. Metabolic abnormalities associated with glycation of LDL include diminished recognition of LDL by the classic LDL receptor; increased covalent binding of LDL in vessel walls ; enhanced uptake of LDL by the macrophages, thus stimulating foam cell formation ; increased platelet aggregation; formation of LDL-immune complexes ; and generation of oxygen free radicals, resulting on oxidative damage to both the lipid and protein components of LDL and to any nearby macromolecules. Oxidized lipoproteins are characterzied by cytotoxicity, potent stimulation of foam cell formation by macrophages, and procoagulant effects. Combined glycation and oxidation, "glycoxidation" occurs when oxidative reactions affect the initial products of glycation, and results in irreversible structural alterations of proteins. Glycoxidation is of greatest significance in long lived proteins such as collagen. In these proteins, glycoxidation products, believed to be atherogenic, accumulate with advancing age : in diabetes, their rate of accumulate is accelerated. Inhibition of glycation, oxidation and glycoxidation may form the basis of future antiaterogenic strategies in both diabetic and nondiabetic individuals.dividuals.

• BMB Reports
• /
• 제51권10호
• /
• pp.486-492
• /
• 2018

The CCN protein family is composed of six matricellular proteins, which serve regulatory roles rather than structural roles in the extracellular matrix. First identified as secreted proteins which are induced by oncogenes, the acronym CCN came from the names of the first three members: CYR61, CTGF, and NOV. All six members of the CCN family consist of four cysteine-rich modular domains. CCN proteins are known to regulate cell adhesion, proliferation, differentiation, and apoptosis. In addition, CCN proteins are associated with cardiovascular and skeletal development, injury repair, inflammation, and cancer. They function either through binding to integrin receptors or by regulating the expression and activity of growth factors and cytokines. Given their diverse roles related to the pathology of certain diseases such as fibrosis, arthritis, atherosclerosis, diabetic nephropathy, retinopathy, and cancer, there are many emerging studies targeting CCN protein signaling pathways in attempts to elucidate their potentials as therapeutic targets.

• 한국버섯학회지
• /
• 제15권1호
• /
• pp.1-7
• /
• 2017

Hydrophobins are surface active proteins that are produced by filamentous fungi including mushrooms. Their ability to self-assemble into an amphipathic membrane at any hydrophilic-hydrophobic interface is most intriguing. These small secreted proteins comprise of eight conserved cysteine residues which form four disulfide bridges and an extraordinary hydrophobic patch. Hydrophobins play critical roles in fungal (and/or mushrooms) growth as structural components and in the interaction of fungi and mushrooms with the environment. The biophysical and biochemical properties of the isolated proteins are remarkable, such as strong adhesion, high surface activity and the formation of various self-assembled structures. With the increasing demands of hydrophobins from fungi and mushroom sources, production and purification in large scale is under challenge. Various applications, ranging from food industries, cosmetics, nanotechnology, biosensors and electrodes, to biomaterials and pharmaceuticals are emerging and a bright future is foreseen.

• BMB Reports
• /
• 제55권7호
• /
• pp.316-322
• /
• 2022

Ubiquitin is relatively modest in size but involves almost entire cellular signaling pathways. The primary role of ubiquitin is maintaining cellular protein homeostasis. Ubiquitination regulates the fate of target proteins using the proteasome- or autophagy-mediated degradation of ubiquitinated substrates, which can be either intracellular or foreign proteins from invading pathogens. Legionella, a gram-negative intracellular pathogen, hinders the host-ubiquitin system by translocating hundreds of effector proteins into the host cell's cytoplasm. In this review, we describe the current understanding of ubiquitin machinery from Legionella. We summarize structural and biochemical differences between the host-ubiquitin system and ubiquitin-related effectors of Legionella. Some of these effectors act much like canonical host-ubiquitin machinery, whereas others have distinctive structures and accomplish non-canonical ubiquitination via novel biochemical mechanisms.

• 한국생물정보학회:학술대회논문집
• /
• 한국생물정보시스템생물학회 2000년도 International Symposium on Bioinformatics
• /
• pp.32-34
• /
• 2000

Computational chemistry is a discipline using computational methods for the calculation of molecular structure, properties, and reaction or for the simulation of molecular behavior. Relating and turning the complexity of data from genomics, high-throughput screening, combinatorial chemical synthesis, gene-expression investigations, pharmacogenomics, and proteomics into useful information and knowledge is the primary goal of bioinformatics. In particular, the structure-based molecular design is one of essential fields in bioinformatics and it can be called as structural bioinformatics. Therefore, the conformational analysis for proteins and peptides using the techniques of computational chemistry is expected to play a role in structural bioinformatics. There are two major computational methods for conformational analysis of proteins and peptides; one is the molecular orbital (MO) method and the other is the force field (or empirical potential function) method. The MO method can be classified into ab initio and semiempirical methods, which have been applied to relatively small and large molecules, respectively. However, the improvement in computer hardwares and softwares enables us to use the ab initio MO method for relatively larger biomolecules with up to v100 atoms or ∼800 basis functions. In order to show how computational chemistry can be used in structural bioinformatics, 1 will present on (1) cis-trans isomerization of proline dipeptide and its derivatives, (2) positional preference of proline in ${\alpha}$-helices, and (3) conformations and activities of Arg-Gly-Asp-containing tetrapeptides.