Chul Won Lee

Chonnam National University

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Hyosuk Yun

Chonnam National University

Jae Il Kim

Seoul National University

Hye Jung Min

Sungkyunkwan University

Song Yub Shin

Chosun University

Jueun Kim

Korea Institute of Materials Science

Sung‐Tae Yang

Chosun University

S. Dinesh Kumar

Chosun University

Kenton J. Swartz

National Institute of Neurological Disorders and Stroke

Jiyoung Nam

Sungkyunkwan University

Sung‐Heui Shin

Chosun University

Cooperative Institutions

Chonnam National University

Yonsei University

Seoul National University

Chosun University

Chonnam National University Hospital

Korea Research Institute of Bioscience and Biotechnology

Gwangju Institute of Science and Technology

Rural Development Administration

Konkuk University

Chungbuk National University

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Solution Structure and Functional Characterization of SGTx1, a Modifier of Kv2.1 Channel Gating^,

Biochemistry (2004)

Chul Won Lee Sung‐Hwan Kim Soung‐Hun Roh Hiroshi Endoh Yoshio Kodera

SGTx1 is a peptide toxin isolated from the venom of the spider Scodra griseipes that has been shown to inhibit outward K+ currents in rat cerebellar granule neurons. Although its amino acid sequence is known to be highly (76%) homologous with that of hanatoxin (HaTx), a well-characterized modifier of Kv2.1 channel gating, the structural and functional characteristics of SGTx1 remain largely unknown. Here we describe the NMR solution structure of SGTx1, the mechanism of its interaction with Kv2.1 channels, and its effect on channel activity once bound. The NMR structure of SGTx1 contains a molecular fold closely resembling the "inhibitor cystine knot" of HaTx, which is composed of an antiparallel β-sheet and four chain reversals stabilized by three disulfide bonds. Functionally, SGTx1 reversibly inhibited K+ currents in oocytes expressing Kv2.1 channels. Moreover, generation of steady-state activation curves showed that, consistent with other gating modifiers, SGTx1 acted by shifting the activation of the channel to more depolarized voltages. Thus, the surface profile and mechanism of action of SGTx1 are similar to those of HaTx. Still, detailed comparison of SGTx1 with HaTx revealed differences in binding affinity and conformational homogeneity that result from differences in the charge distribution at the binding surface and in the amino acid composition of the respective β-hairpin structures in the peptides.

Antiparallel (mathematics)

10.1021/bi0353373

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Citations (94)

Hypothalamic Norepinephrine Mediates Acupunctural effects on the HPA Axis during Ethanol Withdrawal

Zheng Lin Zhao Sang Chan Kim Jie Zhang Hong Feng Liu Bong Hyo Lee

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Cultivation Conditions for Mass Production of an Antifungal Lipopeptide from Bacillus methylotrophicus GH1-13

한국미생물학회 학술대회논문집 (2016)

Jong Min Kim Ki Moon Bong Gong Min Kim Jaekyeong Song Chul Won Lee

Lipopeptide

Bacillus (shape)

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Rattusin structure reveals a novel defensin scaffold formed by intermolecular disulfide exchanges

Scientific Reports (2017)

Hye Jung Min Hyosuk Yun Sehyeon Ji Ganesan Rajasekaran Jae Il Kim

Abstract Defensin peptides are essential for innate immunity in humans and other living systems, as they provide protection against infectious pathogens and regulate the immune response. Here, we report the solution structure of rattusin (RTSN), an α-defensin-related peptide, which revealed a novel C 2 -symmetric disulfide-linked dimeric structure. RTSN was synthesized by solid-phase peptide synthesis (SPPS) and refolded by air oxidation in vitro . Dimerization of the refolded RTSN ( r -RTSN) resulted from five intermolecular disulfide (SS) bond exchanges formed by ten cysteines within two protomer chains. The SS bond pairings of r -RTSN were determined by mass analysis of peptide fragments cleaved by trypsin digestion. In addition to mass analysis, nuclear magnetic resonance (NMR) experiments for a C15S mutant and r -RTSN confirmed that the intermolecular SS bond structure of r -RTSN showed an I-V’, II-IV’, III-III’, IV-II’, V-I’ arrangement. The overall structure of r -RTSN exhibited a cylindrical array, similar to that of β-sandwich folds, with a highly basic surface. Furthermore, fluorescence spectroscopy results suggest that r- RTSN exerts bactericidal activity by damaging membrane integrity. Collectively, these results provide a novel structural scaffold for designing highly potent peptide-based antibiotics suitable for use under various physiological conditions.

10.1038/srep45282

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Citations (18)

Antimicrobial and anti-inflammatory activities of chemokine CXCL14-derived antimicrobial peptide and its analogs

Biochimica et Biophysica Acta (BBA) - Biomembranes (2018)

Ganesan Rajasekaran S. Dinesh Kumar Jiyoung Nam Dasom Jeon Yangmee Kim

CXCL14

Enterococcus faecium

Lipopeptide

10.1016/j.bbamem.2018.06.016

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Citations (54)

Relationship between Leisure Constraints Negotiation, Leisure Satisfaction, and Quality of Life in Professional Soldiers

Journal of Leisure Studies (2012)

정유진 Chul Won Lee Sang Back Nam

Leisure satisfaction

Leisure studies

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Development of Cobalt-Binding Peptide Chelate from Human Serum Albumin: Cobalt-Binding Properties and Stability

International Journal of Molecular Sciences (2022)

Yeonje Cho Armin Mirzapour‐Kouhdasht Hyosuk Yun Jeong Hoon Park Hye Jung Min

Radioactive isotopes are used as drugs or contrast agents in the medical field after being conjugated with chelates such as DOTA, NOTA, DTPA, TETA, CyDTA, TRITA, and DPDP. The N-terminal sequence of human serum albumin (HSA) is known as a metal binding site, such as for Co

Isothermal Titration Calorimetry

Human serum albumin

Alanine

Binding constant

10.3390/ijms23020719

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Citations (4)

A study on Nb-V microalloyed steel for 460 MPa grade H-section columns

Journal of Constructional Steel Research (2020)

Bon Seung Koo Chul Won Lee Young Hoon Lim

Modern trends in high-rise constructions are the use of high-strength hot-rolled section steels with improved impact toughness. The use of higher strength enables architects to use thinner sections and allows achieving a considerable reduction in the total cost of materials. Following the trends, the development of low-carbon steel with a minimum yield strength of 460 MPa has been studied. Alloying elements and process operating conditions were selected to increase strength, elongation, and toughness simultaneously. Two alloying elements, niobium and vanadium, were chosen to enhance strength and impact toughness. Thickness reduction per pass was controlled to perform excessive deformation below the austenite recrystallization stop temperature, and then accelerated cooling has proceeded to obtain grain refinement. Flow stress analysis and microstructure observation have been conducted to cross-validate the effect of precipitation hardening, along with material testing for the evaluation of the mechanical properties.

Recrystallization (geology)

Flow stress

Elongation

Strain hardening exponent

Microalloyed steel

Precipitation hardening

10.1016/j.jcsr.2020.106112

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Citations (5)

Structure of CBP nuclear coactivator binding domain in complex with p53 TAD

Journal of Back and Musculoskeletal Rehabilitation (2010)

Chul Won Lee Maria A. Martinez‐Yamout Helen Dyson Peter E. Wright

10.13018/bmr17073

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Simulations of Allosteric Motions in the Zinc Sensor CzrA

Journal of the American Chemical Society (2011)

Dhruva K. Chakravorty Bing Wang Chul Won Lee David Giedroc Kenneth M. Merz

The zinc sensing transcriptional repressor Staphylococcus aureus CzrA represents an excellent model system to understand how metal sensor proteins maintain cellular metal homeostasis. Zn(II) binding induces a quaternary structural switch from a "closed" conformation to a more "open" conformation, reducing the DNA binding affinity by 4 orders of magnitude. In this study, we use classical molecular dynamics and quantum mechanical/molecular mechanical molecular dynamics simulations to investigate the molecular basis for the large conformational motions and allosteric coupling free energy (∼6 kcal/mol) associated with Zn(II) binding. Our simulations successfully capture the closed to open allosteric switching in DNA bound CzrA on Zn(II) binding. They reveal that zinc binding quenches global conformational sampling by CzrA, whereas DNA binding enhances the mobility of residues in the allosteric metal binding sites. These findings are in close agreement with experiments. We also identify networks of residues involved in correlated and anticorrelated motions that connect the metal binding and DNA binding sites. Our analysis of the essential dynamics shows metal ion binding to be the primary driving force for the quaternary structural change in CzrA. We also show that Zn(II) binding limits the conformational space sampled by CzrA and causes the electrostatic surface potential at the DNA binding interface to become less favorable toward DNA binding. Finally, our simulations provide strong support for a proposed hydrogen-bonding pathway that physically connects the metal binding residue, His97, to the DNA binding interface through the αR helix that is present only in the Zn(II)-bound state. Overall, our simulations provide molecular-level insights into the mechanism of allosteric regulation by CzrA and demonstrate the importance of protein motion in its biological activity.

10.1021/ja208047b

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Citations (46)