Tertiary structure of calcineurin B by homology modeling.
The crystal structure of the calcium-binding protein calmodulin is used to model the immunologically important calcineurin subunit B. The rough structure is produced by computer-aided homology modeling. Refinement of this using molecular dynamics leads to a suggested structure which appears to satisfy reasonable hydrophilicity and hydrogen-bonding criteria. In the absence of a crystal structure, the model may prove useful in modeling of its interactions with the phosphatase catalytic subunit calcineurin A, and help to explain the calcium modulation of this protein.
Dyson Perrins Laboratory, University of Oxford, UK.
S
S
West
P
P
Bamborough
R
R
Tully
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019703:Calcineurin; D002147:Calmodulin / Q000737:chemistry / Q000235:genetics; D002148:Calmodulin-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D003196:Computer Graphics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases