Opioid-binding protein (OBCAM) is rich in β-sheets
Wu, Chuen-Shang C. ; Hasegawa, Junichi ; Smith, Andrew P. ; Loh, Horace H. ; Lee, Nancy M. ; Yang, Jen Tsi
Springer
Published 1990
Springer
Published 1990
| ISSN: |
1573-4943
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|---|---|
| Keywords: |
Opioid-binding proteins ; conformation ; circular dichroism ; sequence-predictive method
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Chemistry and Pharmacology
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| Notes: |
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.
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| Type of Medium: |
Electronic Resource
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| URL: |