Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop

Kyu Song Hyun Kyu Song; Nyung Lee Kee Nyung Lee; Kwon Ki-Sun Kwon; Yu Myeong-Hee Yu; Won Suh Se Won Suh

doi:10.1016/0014-5793(95)01331-8

Crystal structure of an uncleaved α₁-antitrypsin reveals the conformation of its inhibitory reactive loop

Kyu Song Hyun Kyu Song, Nyung Lee Kee Nyung Lee, Kwon Ki-Sun Kwon, Yu Myeong-Hee Yu, Won Suh Se Won Suh

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

The crystal structure of a recombinant human α₁-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 Å data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α₁-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the β-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477].

Original language	English
Pages (from-to)	150-154
Number of pages	5
Journal	FEBS Letters
Volume	377
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(95)01331-8
Publication status	Published - 1995 Dec 18
Externally published	Yes

Keywords

Inhibitory loop
Molecular replacement
Serpin
X-ray structure
α-Antitrypsin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(95)01331-8

Cite this

@article{5f13c0a2853841869aed89c646c9cbf3,

title = "Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop",

abstract = "The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 {\AA} data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the β-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477].",

keywords = "Inhibitory loop, Molecular replacement, Serpin, X-ray structure, α-Antitrypsin",

author = "{Hyun Kyu Song}, {Kyu Song} and {Kee Nyung Lee}, {Nyung Lee} and {Ki-Sun Kwon}, Kwon and {Myeong-Hee Yu}, Yu and {Se Won Suh}, {Won Suh}",

note = "Funding Information: Acknowledgements: We thank the Korea Ministry of Education, Basic Sciences Research Institute Program (S.W.S.), Center for Molecular Catalysis (S.W.S.), and the Korea Ministry of Science and Technology (M.-H.Y., Grant G71142) for financial support. We also thank the Inter-University Center for Natural Science Research Facilities for providing the X-ray equipments. The coordinates will be deposited with the Protein Data Bank.",

year = "1995",

month = dec,

day = "18",

doi = "10.1016/0014-5793(95)01331-8",

language = "English",

volume = "377",

pages = "150--154",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop

AU - Hyun Kyu Song, Kyu Song

AU - Kee Nyung Lee, Nyung Lee

AU - Ki-Sun Kwon, Kwon

AU - Myeong-Hee Yu, Yu

AU - Se Won Suh, Won Suh

N1 - Funding Information: Acknowledgements: We thank the Korea Ministry of Education, Basic Sciences Research Institute Program (S.W.S.), Center for Molecular Catalysis (S.W.S.), and the Korea Ministry of Science and Technology (M.-H.Y., Grant G71142) for financial support. We also thank the Inter-University Center for Natural Science Research Facilities for providing the X-ray equipments. The coordinates will be deposited with the Protein Data Bank.

PY - 1995/12/18

Y1 - 1995/12/18

N2 - The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 Å data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the β-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477].

AB - The crystal structure of a recombinant human α1-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 Å data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central β-sheet A of the uncleaved α1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the β-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477].

KW - Inhibitory loop

KW - Molecular replacement

KW - Serpin

KW - X-ray structure

KW - α-Antitrypsin

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DO - 10.1016/0014-5793(95)01331-8

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VL - 377

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