Structure of FKBP12.6 in complex with rapamycin

FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 Å resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement obse...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2000-03, Vol.56 (3), p.266-271
Main Authors: Deivanayagam, Champion C. S., Carson, Mike, Thotakura, Aruna, Narayana, Sthanam V.L., Chodavarapu, Ramarao S.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
FKBP12.6
Humans
Immunophilins - chemistry
Immunophilins - metabolism
Macromolecular Substances
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
rapamycin
Ryanodine Receptor Calcium Release Channel - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Sirolimus - chemistry
Sirolimus - metabolism
Tacrolimus Binding Proteins
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Summary:FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 Å resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement observed in the helical region of FKBP12.6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2‐binding specificity are presented.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999016571