Opioid-binding protein (OBCAM) is rich in β-sheets

Chuen Shang C. Wu; Junichi Hasegawa; Andrew P. Smith; Horace H. Loh; Nancy M. Lee; Jen Tsi Yang

doi:10.1007/BF01024977

Opioid-binding protein (OBCAM) is rich in β-sheets

Chuen Shang C. Wu, Junichi Hasegawa, Andrew P. Smith, Horace H. Loh, Nancy M. Lee, Jen Tsi Yang

Pharmacology

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Abstract

Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH₂- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23-30 and 83-93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.

Original language	English (US)
Pages (from-to)	3-7
Number of pages	5
Journal	Journal of Protein Chemistry
Volume	9
Issue number	1
DOIs	https://doi.org/10.1007/BF01024977
State	Published - Feb 1990

Keywords

Opioid-binding proteins
circular dichroism
conformation
sequence-predictive method

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10.1007/BF01024977

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title = "Opioid-binding protein (OBCAM) is rich in β-sheets",

abstract = "Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23-30 and 83-93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.",

keywords = "Opioid-binding proteins, circular dichroism, conformation, sequence-predictive method",

author = "Wu, {Chuen Shang C.} and Junichi Hasegawa and Smith, {Andrew P.} and Loh, {Horace H.} and Lee, {Nancy M.} and Yang, {Jen Tsi}",

year = "1990",

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T1 - Opioid-binding protein (OBCAM) is rich in β-sheets

AU - Wu, Chuen Shang C.

AU - Hasegawa, Junichi

AU - Smith, Andrew P.

AU - Loh, Horace H.

AU - Lee, Nancy M.

AU - Yang, Jen Tsi

PY - 1990/2

Y1 - 1990/2

N2 - Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23-30 and 83-93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.

AB - Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23-30 and 83-93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.

KW - Opioid-binding proteins

KW - circular dichroism

KW - conformation

KW - sequence-predictive method

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Opioid-binding protein (OBCAM) is rich in β-sheets

Abstract

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