Molecular cloning and overexpression of the human FK506-binding protein FKBP

Article Abstract:

FK506 is a drug which is very effective in preventing organ transplant rejection, and apparently acts similarly to cyclosporin A by inhibiting events early in the activation of T cells. Activated T cells are responsible for much of the destruction which occurs when a transplanted organ is rejected by its new host. Researchers have found that the cellular protein to which FK506 binds, called FK506 binding protein ( or FKBP), is functionally similar to the protein cyclophilin, which binds cyclosporin A. Researchers have found that both FKBP and cyclophilin are examples of somewhat obscure enzymes called peptidyl-prolyl-cis-trans-isomerases. The gene for FKBP has been cloned and, although functionally similar, FKBP and cyclophilin are structurally unrelated. The role of these unusual enzymes within the cell is not understood, and therefore the mechanism by which FK506 and cyclosporin A act are still to be determined. (Consumer Summary produced by Reliance Medical Information, Inc.)

Physiological aspects, Drug therapy, Graft rejection, Transplantation of organs, tissues, etc., Organ transplantation, Tissue transplantation, Transplantation, Immunosuppressive agents, Cyclosporine, Cyclosporins

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Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex

Article Abstract:

Key cellular processes like gene transcription and DNA replication are facilitated by eukaryotic chromosomes which undergo dynamic assembly and remodelling. A novel ATP-dependent remodelling activity has been identified, and its functional characteristics have been examined. The complex identified has been described as a nucleosome remodelling and deactylating complex. A functional and physical links has been established between nucleosome remodelling proteins and different histone deacetylase chromatin-modifying activities.

Nucleoproteins, Chromosomes

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Regulatory intramolecular association in a tyrosine kinase of the Tec family

Article Abstract:

Multidimensional nuclear magnetic resonance studies reveal the structure of the intramolecular complex formed between the Itk SH3 domain and the adjoining proline-rich ligand, KPLPPTP, confirming that these domains react intramolecularly. This structure represents the first example of an intramolecular interaction between an SH3 domain and a proline-rich ligand. This interaction may characterize the general mechanism which controls the activity of the Tec family kinases

Protein tyrosine kinase, Protein-tyrosine kinase

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