Opioid-binding protein (OBCAM) is rich in beta-sheets.
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.
Wu
C S
CS
Cardiovascular Research Institute, University of California, San Francisco 94143-0524.
Hasegawa
J
J
Smith
A P
AP
Loh
H H
HH
Lee
N M
NM
Yang
J T
JT
D000818:Animals; D002352:Carrier Proteins / Q000648:ultrastructure*; D002417:Cattle; D015815:Cell Adhesion Molecules; D002942:Circular Dichroism; D008562:Membrane Glycoproteins / Q000648:ultrastructure*; D011487:Protein Conformation
D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D008562:Membrane Glycoproteins