Summary
The previously predicted structures of human α-lactalbumin by homology with hen egg white lysozyme by an automatic method, after the alignment stage, are compared to the X-ray determined structure of baboon α-lactalbumin. The root mean square by rotation method (RMSR) deviations for 122 C-α atoms between the two models and the X-ray structure are 2.0 Å and 2.3 Å. The RMSR deviations for all atoms, except for differences in human and baboon sequences, are 2.8 Å and 3.1 Å. If the flexible C-terminus (residues 112–122) are removed then these RMSR deviations are reduced to 2.4 Å and 2.3 Å respectively. These results are consistent with the fact that the RMSR deviation between the human and baboon X-ray structures increases from residue 112 onwards and is conformationally flexible.
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Robson, B., Platt, E. Comparison of the X-ray structure of baboon α-lactalbumin and the tertiary predicted computer models of human α-lactalbumin. J Computer-Aided Mol Des 4, 369–379 (1990). https://doi.org/10.1007/BF00117402
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DOI: https://doi.org/10.1007/BF00117402