1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

Hiroyuki Hanzawa; Ichio Shimada; Takashi Kuzuhara; Hiroto Komano; Daisuke Kohda; Fuyuhiko Inagaki; Shunji Natori; Yoji Arata

doi:10.1016/0014-5793(90)81206-4

¹H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

Hiroyuki Hanzawa, Ichio Shimada, Takashi Kuzuhara, Hiroto Komano, Daisuke Kohda, Fuyuhiko Inagaki, Shunji Natori, Yoji Arata

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

90 Citations (Scopus)

Abstract

The solution conformation of an antibacterial protein sapecin has been determined by ¹H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.

Original language	English
Pages (from-to)	413-420
Number of pages	8
Journal	FEBS Letters
Volume	269
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(90)81206-4
Publication status	Published - Sept 3 1990
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(90)81206-4

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title = "1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin",

abstract = "The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.",

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T1 - 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

AU - Hanzawa, Hiroyuki

AU - Shimada, Ichio

AU - Kuzuhara, Takashi

AU - Komano, Hiroto

AU - Kohda, Daisuke

AU - Inagaki, Fuyuhiko

AU - Natori, Shunji

AU - Arata, Yoji

PY - 1990/9/3

Y1 - 1990/9/3

N2 - The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.

AB - The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.

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¹H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

Abstract

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