Title : Crystal structures of the free and ligand-bound FK1-FK2 domain segment of FKBP52 reveal a flexible inter-domain hinge.

Pub. Date : 2013 Nov 15

PMID : 23933011






3 Functional Relationships(s)
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1 The immunophilin FKBP52 is composed of three domains, an FK506-binding domain with peptidyl-prolyl isomerase activity, an FKBP-like domain of unknown function and a TPR-clamp domain, which recognizes the C-terminal peptide of Hsp90 with high affinity. Tacrolimus FKBP prolyl isomerase 4 Homo sapiens
2 The herein reported crystal structures of FKBP52 reveal that the short linker connecting the FK506-binding domain and the FKBP-like domain acts as a flexible hinge. Tacrolimus FKBP prolyl isomerase 4 Homo sapiens
3 We further present two co-crystal structures of FKBP52 in complex with the prototypic ligand FK506 and a synthetic analog thereof. Tacrolimus FKBP prolyl isomerase 4 Homo sapiens