FKBP52

1N1A, 1P5Q, 1Q1C, 1QZ2, 4DRJ, 4LAV, 4LAW, 4LAX, 4LAY, 4TW8228814228ENSG00000004478ENSMUSG00000030357Q02790P30416NM_002014NM_010219NP_002005NP_034349FK506-binding protein 4 is a protein that in humans is encoded by the FKBP4 gene.1n1a: Crystal Structure of the N-terminal domain of human FKBP521p5q: Crystal Structure of FKBP52 C-terminal Domain1q1c: Crystal structure of N(1-260) of human FKBP521qz2: Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp901rot: STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE1rou: STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, 22 STRUCTURES FK506-binding protein 4 is a protein that in humans is encoded by the FKBP4 gene. The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. This protein contains TPR repeats and has a PPlase domain. Recent research suggests that FKBP52 may play a role in preventing the Tau protein from turning pathogenic. This may prove significant for the development of new Alzheimer's drugs and for detecting the disease before the onset of clinical symptoms. FKBP52 has been shown to interact with GLMN.