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홈 > 간행물 권호
  • 발행기관: 한국구조생물학회
  • 간행물:
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Biodesign(Biodesign)

  • 발행기관 : 한국구조생물학회(Korean Society for Structural Biology)
  • 출처구분 : 학회
  • 간행물유형 : 학술저널
  • 발행주기 : 계간 (발행월:3,6,9,12)
  • Print ISSN : 2288-6982
  • Online ISSN : 2288-7105
  • 등재정보 : KCI 등재후보
Biodesign
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Accurate protein structure prediction: what comes next?
Accurate protein structure prediction: what comes next?
Chaok Seok;Minkyung Baek;Martin Steinegger;Hahnbeom Park;Gyu Rie Lee;Jonghun Won
한국구조생물학회 / Biodesign Vol 9, No 3, Sep / 2021 / 47-50 (4 pages)
자연과학>생물학 / KDC : 순수과학 > 생물과학 / KCI : 자연과학 > 생물학
초록보기
Protein structure prediction has become extremely accurate, and its results are now comparable with those of experimental methods for a large number of proteins. However, there remain some technical hurdles to clear before the current structure prediction tools can be directly applied to a wide range of biomedical problems. New perspectives on future developments in the area of structure prediction and its biomedical applications are presented.
Purification, crystallization, and X-ray crystallographic analysis of Acetolactate synthase from Hydrogenobacter thermophilus
Purification, crystallization, and X-ray crystallographic analysis of Acetolactate synthase from Hydrogenobacter thermophilus
Ji-Won Kim;Jeong-Sun Kim
한국구조생물학회 / Biodesign Vol 9, No 3, Sep / 2021 / 51-54 (4 pages)
자연과학>생물학 / KDC : 순수과학 > 생물과학 / KCI : 자연과학 > 생물학
초록보기
Acetolactate synthase (ALS) catalyzes the chemical reaction in plants and microorganisms that converts two pyruvate molecules to an acetolactate molecule and a carbon dioxide. To confer change on its substrate specificity for one carbon chemicals, structural study was initiated. For this, the recombinant ALS protein from Hydrogenobacter thermophilus (HtALS) was expressed in Escherichia coli , and homogeneously purified. The purified HtALS protein was crystallized from the precipitant composed of 0.3 M Ammonium sulfate, 0.1 M Sodium cacodylate (pH 6.5), and 18% (w/v) polyethylene glycol 4000. Diffraction data was collected to 2.4 Å resolution. The crystal belongs to the primitive orthorhombic P212121 space group with unit-cell parameters a = 75.24 Å, b = 76.62 Å, c = 194.69 Å, and α = β = γ = 90°. There are two HtALS molecules in the asymmetric unit.
Purification, crystallization and X-ray crystallographic analysis of RPTPH
Purification, crystallization and X-ray crystallographic analysis of RPTPH
Myeongbin Kim;Seong Eon Ryu
한국구조생물학회 / Biodesign Vol 9, No 3, Sep / 2021 / 55-58 (4 pages)
자연과학>생물학 / KDC : 순수과학 > 생물과학 / KCI : 자연과학 > 생물학
초록보기
Receptor-type protein tyrosine phosphatases (RPTPs) belong to the protein tyrosine phosphatase (PTP) family and play a critical role in cell signaling. RPTPH, a type of RPTP, consists of long extracellular domains, a transmembrane domain, and a single intracellular domain with phosphatase activity. RPTPH is involved in phosphorylation of target proteins involved in the AKT signaling pathway and regulates T-cell function and cell apoptosis. The protein is also implicated in progression of colorectal and lung cancers. Despite the importance of RPTPH in tumor-related cell signaling and therapeutic drug development, the structure of this enzyme has not yet been determined. We overexpressed, purified, and crystallized the catalytic domain of RPTPH. The RPTPH crystal diffracted at a resolution of 1.56 Å. It belonged to the space group P32 with unit cell parameters a = b = 56.46 Å, c = 80.45 Å, α = β = 90°, and γ = 120°.