Relative-residue surface-accessibility patterns reveal myoglobin and catalase similarity.
A novel sliding-window search method using relative-residue surface-accessibility patterns identified extensive, but unsuspected, structural similarity over a 3-helix region in the C-terminus of the evolutionarily unrelated proteins sperm-whale myoglobin and beef liver catalase. This clear example of structural similarity between non-homologous proteins highlights the importance of relative-residue surface-accessibility patterns in understanding the local folded structure in proteins.
Cockcroft
V B
VB
Molecular Graphics Unit, Bath University, UK.
Osguthorpe
D J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D002374:Catalase / Q000737:chemistry* / Q000235:genetics; D002417:Cattle; D008099:Liver / Q000201:enzymology; D008297:Male; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D016415:Sequence Alignment; D013094:Spermatozoa / Q000737:chemistry; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013499:Surface Properties; D014907:Whales
D009211:Myoglobin; D002374:Catalase