Structural highlights
Function
[FKB1B_HUMAN] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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.
Structure of FKBP12.6 in complex with rapamycin.,Deivanayagam CC, Carson M, Thotakura A, Narayana SV, Chodavarapu RS Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):266-71. PMID:10713512[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deivanayagam CC, Carson M, Thotakura A, Narayana SV, Chodavarapu RS. Structure of FKBP12.6 in complex with rapamycin. Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):266-71. PMID:10713512
