• Journal of the Korean Magnetic Resonance Society
• /
• v.14 no.2
• /
• pp.127-133
• /
• 2010

Redox-dependent conformational change of human 8-kDa Dynein light chain (LC8) plays important role in regulating NF-${\kappa}B$ signaling pathway. In this study we characterized the structural states of the oxidized and reduced forms of LC8 by using NMR spectroscopy. The $^1H-^{15}N$ 2D HSQC spectra of oxidized LC8 indicated that no significant change in tertiary structure of LC8 occurred upon oxidation. The chemical shift perturbations of LC8 upon oxidation suggest a redox-dependent quaternary structural change.

• Journal of Microbiology and Biotechnology
• /
• v.22 no.12
• /
• pp.1724-1730
• /
• 2012

An ${\alpha}$-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the enzymatic characterization and structural analysis of TmAFase. Tight domain associations found in TmAFase, such as an inter-domain disulfide bond (Cys306 and Cys476) in each monomer, a novel extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) was identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates.

• BMB Reports
• /
• v.42 no.7
• /
• pp.411-417
• /
• 2009

Transcriptional activation domain (TAD) in virion protein 16 (VP16) of herpes simplex virus does not have any globular structure, yet exhibits a potent transcriptional activity. In order to probe the structural basis for the transcriptional activity of VP16 TAD, we have used NMR spectroscopy to investigate its detailed structural features. Results show that an unbound VP16 TAD is not merely "unstructured" but contains four short motifs (residues 424-433, 442-446, 465-467 and 472-479) with transient structural order. Pre-structured motifs in other intrinsically unfolded proteins (IUPs) were shown to be critically involved in target protein binding. The 472-479 motif was previously shown to bind to $hTAF_{II}31$, whereas the $hTAF_{II}31$-binding ability of other motifs found in this study has not been addressed. The VP16 TAD represents another IUP whose pre-structured motifs mediate promiscuous binding to various target proteins.

• Proceedings of the Korean Biophysical Society Conference
• /
• 2003.06a
• /
• pp.63-63
• /
• 2003

$\alpha$$_1$-Antityrpsin is a member of the serine protease inhibitor (SERPIN) family that shares a common tertiary structure. The reactive site loop (RSL) of serpins is exposed at one end of the molecule for protease binding. Upon cleavage by a target protease, the RSL is inserted into the major $\beta$-sheet A, which is a necessary process for formation of a tight inhibitory complex. Various biochemical and structural studies suggest that the rate of the RSL insertion upon binding a target protease is critical for inhibitory activity, and it is thought that helix F region (thFs3A and helix F) located in front of $\beta$-sheet A, should be lifted for the loop insertion during complex formation.

• Proceedings of the Korean Magnetic Resonance Society Conference
• /
• 2002.08a
• /
• pp.76-76
• /
• 2002

• Journal of the Korea Academia-Industrial cooperation Society
• /
• v.11 no.3
• /
• pp.971-977
• /
• 2010

A flood of biological data has caused many challenges in computing. Bioinformatics, the application of computational techniques to analyze the information associated with biomolecules on a large-scale, has now firmly established itself as an interdisciplinary subject in molecular biology, and encompasses a wide range of subject areas from structural biology, genomics, proteomics, systems biology, biostatistics to computer science. In this review, I provide an introduction and overview of the current state of bioinformatics. Looking at the types of biological information and databases that are commonly used, I also deals with some of bioinformatics application domains which are closely related to areas of computer science.

• Molecules and Cells
• /
• v.19 no.2
• /
• pp.157-166
• /
• 2005

Transfer RNA (tRNA) is a key molecule to decode the genetic information on mRNA to amino aicds (protein), in a ribosome. For tRNA to fulfill its adopter function, tRNA should be processed into the standard length, and be post-transcriptionally modified. This modification step is essential for the tRNA to maintain the canonical L-shaped structure, which is required for the decoding function of tRNA. Otherwise, it has recently been proposed that modification procedure itself contributes to the RNA (re)folding, where the modification enzymes function as a kind of RNA chaperones. Recent genome analyses and post-genome (proteomics and transcriptomics) analyses have identified genes involved in the tRNA processings and modifications. Furthermore, post-genomic structural analysis has elucidated the structural basis for the tRNA maturation mechanism. In this paper, the recent progress of the structural biology of the tRNA processing and modification is reviewed.

• The KIPS Transactions:PartD
• /
• v.8D no.5
• /
• pp.553-560
• /
• 2001

Bioinformatics is a discipline to support biological experiment projects by storing, managing data arising from genome research. In can also lead the experimental design for genome function prediction and regulation. Among various approaches of the genome research, the proteomics have been drawing increasing attention since it deals with the final product of genomes, i.e., proteins, directly. This paper proposes a data mining technique to predict the structural characteristics of a given protein group, one of dominant factors of the functions of them. After explains associations among amino acid subsequences in the primary structures of proteins, which can provide important clues for determining secondary or tertiary structures of them, it defines a sequence association rule to represent the inter-subsequences. It also provides support and confidence measures, newly designed to evaluate the usefulness of sequence association rules, After is proposes a method to discover useful sequence association rules from a given protein group, it evaluates the performance of the proposed method with protein sequence data from the SWISS-PROT protein database.

• Genomics & Informatics
• /
• v.1 no.2
• /
• pp.65-74
• /
• 2003

Data mining differs primarily from traditional data analysis on an important dimension, namely the scale of the data. That is the reason why not only statistical but also computer science principles are needed to extract information from large data sets. In this paper we briefly review data mining, its characteristics, typical data mining algorithms, and potential and ongoing applications of data mining at biopharmaceutical industries. The distinguishing characteristics of data mining lie in its understandability, scalability, its problem driven nature, and its analysis of retrospective or observational data in contrast to experimentally designed data. At a high level one can identify three types of problems for which data mining is useful: description, prediction and search. Brief review of data mining algorithms include decision trees and rules, nonlinear classification methods, memory-based methods, model-based clustering, and graphical dependency models. Application areas covered are discovery compound libraries, clinical trial and disease management data, genomics and proteomics, structural databases for candidate drug compounds, and other applications of pharmaceutical relevance.

• BMB Reports
• /
• v.45 no.12
• /
• pp.693-699
• /
• 2012

Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enabling us to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context.