Abstract:
:We propose a general classification scheme for loops, aperiodic segments of protein structure. In an effort to avoid the geometric complexity created by non-repeating phi psi angles, a morphologic definition that focuses upon the linearity and planarity of loops is utilized. Out of 432 loops (4 to 20 residues in length) extracted from 67 proteins, 205 are classified as linear (straps), 133 as non-linear and planar (omegas), and 86 as non-linear and non-planar (zetas). The remaining 8 are classified as compound loops because they contain a combination of strap, omega, and zeta morphologies. We introduce a structural alphabet as a shorthand notation for describing local conformation. The symbols of this alphabet are based on the virtual dihedral angle joining four consecutive alpha carbons. The notation is used to provide a compact description of loop motifs in phosphate binding and calcium binding proteins. Since similar loop conformations form similar "words", the structural sequence facilitates the search for common structural motifs in a family of loops. Contrary to the view of loops as "random coils", we find loops to have positional preferences for amino acid residues analogous to those previously described for beta-turns.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Ring CS,Kneller DG,Langridge R,Cohen FEdoi
10.1016/0022-2836(92)90553-vkeywords:
subject
Has Abstractpub_date
1992-04-05 00:00:00pages
685-99issue
3eissn
0022-2836issn
1089-8638pii
0022-2836(92)90553-Vjournal_volume
224pub_type
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