CuTLat - curvature, twist, lateral bending

HEAT repeats in Importin-Beta. See publication for further details, please.

CuTLat determines inter-repeat curvature, twist and lateral bending angles, as well as their full-length sums for multi-repeat unit proteins, including e.g. LRR, Armadillo, HEAT or ankyrin repeat proteins. As the principal axes of repeats are used for the calculation of inter-repeat angles, a prior selection of specific conserved reference groups is not required.

CuTLat is useful for comparing the structural differences of protein states bound to different binding partners, of different crystal forms or of orthologues. CuTLat can also be used to monitor the structural changes of highly flexible repeat proteins during molecular dynamics simulations. As input, only a data file containing the start and stop residues of repeat units and a pdb file are needed.


Forwood, J. K.; Lange, A.; Zachariae, U.; Marfori, M.; Preast, C.; Grubmüller, H.; Stewart, M.; Corbett, A. H.; Kobe, B.: Quantitative structural analysis of importin-β flexibility: Paradigm for solenoid protein structures. Structure 18 (9), pp. 1171 - 1183 (2010)
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