Opioid-binding protein (OBCAM) is rich in beta-sheets
| Autor: | Nancy M. Lee, Jen Tsi Yang, Andrew P. Smith, Horace H. Loh, Jun-Ichi Hasegawa, Chuen Shang C. Wu |
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| Rok vydání: | 1990 |
| Předmět: |
Circular dichroism
Membrane Glycoproteins biology Cell adhesion molecule Stereochemistry Chemistry Protein Conformation Binding protein Circular Dichroism Sequence (biology) Adhesion Biochemistry Amphiphile biology.protein Bioorganic chemistry Animals Cattle Antibody Carrier Proteins Cell Adhesion Molecules |
| Zdroj: | Journal of protein chemistry. 9(1) |
| ISSN: | 0277-8033 |
| Popis: | Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half beta-sheets and one fourth alpha-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 beta-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 amphipathic beta-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding. |
| Databáze: | OpenAIRE |
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