Disulfide pairings and secondary structure of porcine β-microseminoprotein

Iren Wang; Tsun Ai Yu; Shih Hsiung Wu; Wen Chang Chang; Chinpan Chen

doi:10.1016/S0014-5793(03)00308-9

Disulfide pairings and secondary structure of porcine β-microseminoprotein

Iren Wang, Tsun Ai Yu, Shih Hsiung Wu, Wen Chang Chang, Chinpan Chen

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

11 Citations (Scopus)

Abstract

A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine β-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations. Surprisingly, our derived pairings differ from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel β-sheets. As we know, this is the first detailed secondary structure reported among several types of MSPs.

Original language	English
Pages (from-to)	80-84
Number of pages	5
Journal	FEBS Letters
Volume	541
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00308-9
Publication status	Published - Apr 24 2003
Externally published	Yes

Keywords

Human prostate secretory protein of 94 amino acids
Na,K-adenosine triphosphatase inhibitor
Nuclear magnetic resonance
Structure
β-Microseminoprotein

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)00308-9

Cite this

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title = "Disulfide pairings and secondary structure of porcine β-microseminoprotein",

abstract = "A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine β-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations. Surprisingly, our derived pairings differ from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel β-sheets. As we know, this is the first detailed secondary structure reported among several types of MSPs.",

keywords = "Human prostate secretory protein of 94 amino acids, Na,K-adenosine triphosphatase inhibitor, Nuclear magnetic resonance, Structure, β-Microseminoprotein",

author = "Iren Wang and Yu, {Tsun Ai} and Wu, {Shih Hsiung} and Chang, {Wen Chang} and Chinpan Chen",

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T1 - Disulfide pairings and secondary structure of porcine β-microseminoprotein

AU - Wang, Iren

AU - Yu, Tsun Ai

AU - Wu, Shih Hsiung

AU - Chang, Wen Chang

AU - Chen, Chinpan

PY - 2003/4/24

Y1 - 2003/4/24

N2 - A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine β-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations. Surprisingly, our derived pairings differ from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel β-sheets. As we know, this is the first detailed secondary structure reported among several types of MSPs.

AB - A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine β-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations. Surprisingly, our derived pairings differ from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel β-sheets. As we know, this is the first detailed secondary structure reported among several types of MSPs.

KW - Human prostate secretory protein of 94 amino acids

KW - Na,K-adenosine triphosphatase inhibitor

KW - Nuclear magnetic resonance

KW - Structure

KW - β-Microseminoprotein

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ER -

Disulfide pairings and secondary structure of porcine β-microseminoprotein

Abstract

Keywords

ASJC Scopus subject areas

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