3o5q | pdb_00003o5q

Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO

spinqualitylabelsall models 3o5q, resolution 0.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o5q is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DMS Related: 3o5d, 3o5e, 3o5f, 3o5g, 3o5i, 3o5j, 3o5k, 3o5l, 3o5m, 3o5o, 3o5p, 3o5r, 1kt0 Gene: AIG6, FKBP5, FKBP51 (HUMAN) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FKBP5_HUMAN] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP. Publication Abstract from PubMed Steroid hormone receptors are key components of mammalian stress and sex hormone systems. Many of them rely on the Hsp90 chaperone system for full function and are further fine-tuned by Hsp90-associated peptidyl-prolyl isomerases such as FK506-binding proteins 51 and 52. FK506-binding protein 51 (FKBP51) has been shown to reduce glucocorticoid receptor signalling and has been genetically associated with human stress resilience and with numerous psychiatric disorders. The peptidyl-prolyl isomerase domain of FKBP51 contains a high-affinity binding site for the natural products FK506 and rapamycin and has further been shown to convey most of the inhibitory activity on the glucocorticoid receptor. FKBP51 has therefore become a prime new target for the treatment of stress-related affective disorders that could be amenable to structure-based drug design. Here, a series of high-resolution structures of the peptidyl-prolyl isomerase domain of FKBP51 as well as a cocrystal structure with the prototypic ligand FK506 are described. These structures provide a detailed picture of the drug-binding domain of FKBP51 and the molecular binding mode of its ligand as a starting point for the rational design of improved inhibitors. Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.,Bracher A, Kozany C, Thost AK, Hausch F Acta Crystallogr D Biol Crystallogr. 2011 Jun;67(Pt 6):549-59. Epub 2011 May 17. PMID:21636895 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also FK506 binding protein

Proteopedia Page Contributors and Editors (what is this?)

OCA