Striking sequence similarity among sialic acid-binding lectin, pancreatic ribonucleases, and angiogenin: possible structural and functional relationships.
We found that a sialic acid-binding lectin (SABL) from bullfrog egg bears a remarkable degree of similarity with human angiogenin and the pancreatic ribonucleases (EC 3.1.27.5). Based on (1) the conservation of several disulfide bond-forming cysteines, (2) a cluster of nonpolar residues, and (3) a number of active-site residues of bovine ribonuclease, we propose that SABL has essentially the same secondary and tertiary structures and very likely has ribonuclease activity. Other possible physiological roles are discussed.
Lewis
M T
MT
National Biomedical Research Foundation, Georgetown University Medical Center, Washington, DC 20007.
Hunt
L T
LT
Barker
W C
WC
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003627:Data Interpretation, Statistical; D006801:Humans; D037102:Lectins / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D011898:Ranidae; D012259:Ribonuclease, Pancreatic / Q000235:genetics / Q000378:metabolism; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; D013329:Structure-Activity Relationship; D014426:Turtles
D037102:Lectins; D011506:Proteins; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; C046366:angiogenin; D012259:Ribonuclease, Pancreatic