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.
West
S
S
Dyson Perrins Laboratory, University of Oxford, UK.
Bamborough
P
P
Tully
R
R
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