Automatic definition of recurrent local structure motifs in proteins.
An automatic procedure for defining recurrent folding motifs in proteins of known structure is described. These motifs are formed by short polypeptide fragments of equal size containing between four and seven residues. The method applies a classical clustering algorithm that operates on distances between selected backbone atoms. In one application, we use it to cluster all protein fragments into only four structural classes. This classification is rough considering the observed diversity of local structures, but comparable in homogeneity to the four classes of secondary structure (alpha-helix, beta-strand, turn and coil). Yet, it discriminates between extended and curved coil and distinguishes beta-bulges from beta-strands. In a second application, the clustering procedure is combined with assignment of backbone dihedral angles to allowed regions in the Ramachandran map. This produces an exhaustive repertoire of highly homogeneous families of structural motifs that contains all the beta-hairpins, beta alpha- and alpha beta-loops previously defined by manual procedures, and new structural families of which two examples, a beta alpha-loop and an alpha-helix beginning, are analyzed in detail. The described automatic procedures should be useful in categorizing structure information in proteins, thereby increasing our ability to analyze relations between structure and sequence.
Rooman
M J
MJ
Unité de Conformation des Macromolécules Biologiques, Université Libre de Bruxelles, Belgium.
Rodriguez
J
J
Wodak
S J
SJ
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010741:Phospholipases A; D011487:Protein Conformation; D011506:Proteins
D011506:Proteins; D010741:Phospholipases A