A critical evaluation of the predicted and X-ray structures of alpha-lactalbumin.
The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine alpha-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon alpha-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on C alpha s of residues 1-95, 1.1 A).
Acharya
K R
KR
Laboratory of Molecular Biophysics, University of Oxford, England.
Stuart
D I
DI
Phillips
D C
DC
Scheraga
H A
HA
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D003198:Computer Simulation; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010215:Papio; D011392:Proline / Q000032:analysis; D011487:Protein Conformation; D013045:Species Specificity; D014961:X-Ray Diffraction
D007768:Lactalbumin; D011392:Proline; D002118:Calcium