The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins.
The amino-acid sequence from the bilin binding protein (BBP) of the butterfly Pieris brassicae has been determined. The apoprotein with a length of 173 amino-acid residues has a molecular mass of 19,676 Da. The sequence analysis was performed by automated Edman degradation of the intact apoprotein and of fragments as large as possible generated from different digestions. The 3-dimensional structure of BBP, determined by Huber et al. (Huber, R., Schneider, M., Epp, O., Mayr, I., Messerschmidt, A., Pflugrath, J. & Kayser, H. (1987) J. Mol. Biol. 195, 423-434 and Huber, R., Schneider, M., Mayr, I., Müller, R., Deutzmann, R., Suter, F., Zuber, H., Falk, H. & Kayser, H. (1987) J. Mol. Biol. 198, 499-513) down to 2-A resolution, exhibits a similar conformation to the human retinol binding protein. Sawyer (Sawyer, L. (1987) Nature (London) 327, 659) demonstrated that proteins from a wide variety of sources can be gathered into a "superfamily". Computer searches of data banks yielded in a new member of this superfamily, namely human alpha 1-acid glycoprotein. One of the functions of the listed proteins is to bind and transport small hydrophobic molecules in serum.
Suter
F
F
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Kayser
H
H
Zuber
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002080:Butterflies / Q000378:metabolism*; D002352:Carrier Proteins / Q000097:blood / Q000235:genetics*; D006801:Humans; D019476:Insect Proteins; D007915:Lepidoptera / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012177:Retinol-Binding Proteins / Q000235:genetics*; D013045:Species Specificity
D002352:Carrier Proteins; D019476:Insect Proteins; D012177:Retinol-Binding Proteins; C053849:bilin-binding protein, insect