Pub. Date : 2007 Aug 31
PMID : 17606610
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Hyperphosphorylation at a single amino acid residue, Ser-2808, has been proposed to directly disrupt the binding of a 12.6-kDa FK506-binding protein (FKBP12.6) to RyR2, causing a RyR2 malfunction that triggers cardiac arrhythmias in human heart failure. | Serine | FKBP prolyl isomerase 1B | Homo sapiens |
| 2 | Hyperphosphorylation at a single amino acid residue, Ser-2808, has been proposed to directly disrupt the binding of a 12.6-kDa FK506-binding protein (FKBP12.6) to RyR2, causing a RyR2 malfunction that triggers cardiac arrhythmias in human heart failure. | Serine | FKBP prolyl isomerase 1B | Homo sapiens |
| 3 | To determine the structural basis of the interaction between Ser-2808 and FKBP12.6, we have employed two independent approaches to map this phosphorylation site in RyR2 by three-dimensional cryo-electron microscopy. | Serine | FKBP prolyl isomerase 1B | Homo sapiens |
| 4 | Importantly, the three-dimensional location of the Ser-2808 phosphorylation site is 105-120 A distance from the FKBP12.6 binding site mapped previously, indicating that Ser-2808 is unlikely to be directly involved in the binding of FKBP12.6 to RyR2, as had been proposed previously. | Serine | FKBP prolyl isomerase 1B | Homo sapiens |