Title : Structural characterization of the RyR1-FKBP12 interaction.

Pub. Date : 2006 Mar 3

PMID : 16405911






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Removal of FKBP12 using FK506 or rapamycin causes an increased open probability and an increase in the frequency of sub-conductance states in RyR1. Tacrolimus ryanodine receptor 1 Homo sapiens
2 The orientation of RyR1-bound FKBP12, with part of its FK506 binding site facing towards RyR1, allows us to propose how FK506 is involved in the dissociation of FKBP12 from RyR1. Tacrolimus ryanodine receptor 1 Homo sapiens
3 The orientation of RyR1-bound FKBP12, with part of its FK506 binding site facing towards RyR1, allows us to propose how FK506 is involved in the dissociation of FKBP12 from RyR1. Tacrolimus ryanodine receptor 1 Homo sapiens
4 The orientation of RyR1-bound FKBP12, with part of its FK506 binding site facing towards RyR1, allows us to propose how FK506 is involved in the dissociation of FKBP12 from RyR1. Tacrolimus ryanodine receptor 1 Homo sapiens
5 The orientation of RyR1-bound FKBP12, with part of its FK506 binding site facing towards RyR1, allows us to propose how FK506 is involved in the dissociation of FKBP12 from RyR1. Tacrolimus ryanodine receptor 1 Homo sapiens