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Variable Domain Torsion Angles

Immunoglobulin variable domains contain a number of positions with conserved positive Phi angles. Most, but not all of these positions show a strong preferences for Gly. Other residue types may have a destabilizing effect in those positions. VL kappa domains usually also contain two cis-prolines. cis-Pro L8 forms the "kink" in framework I. S.Spada et al. have shown that replacement of this cis-Pro by other residue types has a destabilizing effect. A similar cis-Pro is present in the equivalent position of many T-cell receptor variable domains. VL lambda and heavy chain variable domains have a one-residue deletion compared to VL kappa and do not contain conserved cis-prolines in the FR1 kink. A second conserved cis-Pro in Position L136 is responsible for the omega-loop conformation of the CDR 3 of most of the kappa domains

VL Positions with conserved positive Phi Angles or cis Peptide Bonds

VH Positions with conserved positive Phi Angles or cis Peptide Bonds

VL Positions with conserved positive Phi Angles or cis Peptide Bonds

VH Positions with conserved positive Phi Angles or cis Peptide Bonds

Things to come: Ramachandran plot by residue number

AAAAA Homepage Zürich University Dept. of Biochemistry Plückthun Group Annemarie Honegger

Last Modified by A.Honegger Wednesday, January 26, 2005