Prediction of prolyl residues in cis-conformation in protein structures on the basis of the amino acid sequence.
In proteins most peptide bonds are in trans-conformation: the torsion angle omega = 180 degrees. Only few show cis-conformation in known protein structures (omega = 0 degrees). Most of them are prolyl residues. About 6% of about 4000 prolyl residues are in cis-conformation. Between trans- and cis-prolyl residues significant differences are observed in the surrounding sequences. E.g. there are large amounts of aromatic residues N-terminally in case of cis-prolyl residues, but in the case of trans-prolyl residues more aromatic amino acids occur C-terminally. But in all cases there are only complex patterns which are indicative of cis- and trans-conformation, respectively. Considering the neighbours (+/- 6 residues) of prolyl residues and their physicochemical properties we find 6 different patterns which allow one to assign correctly about 75% of known cis-structured prolyl residues, whereby no false positive one is predicted.
Frömmel
C
C
Free University Berlin, Germany.
Preissner
R
R
D003461:Crystallography; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011392:Proline; D011487:Protein Conformation; D011506:Proteins / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
D011506:Proteins; D011392:Proline