FKBP: Difference between revisions

Latest revision as of 03:40, 13 February 2025

FKBP[edit]

Cartoon representation of FKBP protein structure

FKBP, or FK506-binding protein, is a family of proteins that have a high affinity for the immunosuppressive drug Tacrolimus (also known as FK506). These proteins are characterized by their ability to bind to immunophilins and are involved in various cellular processes, including protein folding and trafficking.

Structure[edit]

FKBP proteins are known for their peptidyl-prolyl isomerase (PPIase) activity, which catalyzes the cis-trans isomerization of proline residues in polypeptide chains. This activity is crucial for proper protein folding and function. The structure of FKBP proteins typically includes a conserved FKBP domain, which is responsible for their binding activity.

Function[edit]

The primary function of FKBP proteins is to assist in protein folding and to act as molecular chaperones. They are also involved in the regulation of cell signaling pathways. FKBP12, one of the most studied members of this family, binds to the calcium release channel ryanodine receptor and modulates its activity.

Clinical Significance[edit]

FKBP proteins are significant in the field of immunology due to their role in the mechanism of action of immunosuppressive drugs like Tacrolimus. By binding to FKBP, Tacrolimus inhibits the activity of calcineurin, a phosphatase involved in T-cell activation, thereby suppressing the immune response. This makes FKBP proteins a target for therapeutic interventions in organ transplantation and autoimmune diseases.

Related pages[edit]

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-'''FKBP''' (FK506 binding protein) is a family of [[protein]]s that are known for their ability to bind to the [[immunosuppressive]] drugs FK506 (tacrolimus) and rapamycin. They are found in a wide range of organisms, from bacteria to humans, and play a variety of roles in cellular processes.
+== FKBP ==
-== Function ==
+[[File:Fkbp-cartoon-1fkj.png|thumb|right|Cartoon representation of FKBP protein structure]]
-FKBPs are part of the larger family of [[immunophilin]]s, which also includes the cyclophilins. They are characterized by their ability to bind to immunosuppressive drugs, but they also have other functions. For example, they are involved in protein folding, signal transduction, and the regulation of apoptosis.
+FKBP, or FK506-binding protein, is a family of proteins that have a high affinity for the immunosuppressive drug [[Tacrolimus]] (also known as FK506). These proteins are characterized by their ability to bind to [[immunophilin]]s and are involved in various cellular processes, including protein folding and trafficking.
-FKBPs have a conserved domain, known as the FKBP-type peptidyl-prolyl cis-trans isomerase domain. This domain allows them to catalyze the interconversion of the cis and trans isomers of proline residues in proteins, which is a critical step in protein folding.
+== Structure ==
-== Clinical significance ==
+FKBP proteins are known for their peptidyl-prolyl isomerase (PPIase) activity, which catalyzes the cis-trans isomerization of proline residues in polypeptide chains. This activity is crucial for proper protein folding and function. The structure of FKBP proteins typically includes a conserved FKBP domain, which is responsible for their binding activity.
-FKBPs are the target of several immunosuppressive drugs, including FK506 and rapamycin. These drugs bind to the FKBP protein and then inhibit the activity of a protein called calcineurin, which is involved in the activation of T cells. This makes them useful in preventing organ rejection after transplantation.
+== Function ==
-In addition, mutations in FKBP genes have been associated with several diseases. For example, mutations in the FKBP10 gene can cause a form of osteogenesis imperfecta, a disorder that affects the bones.
+The primary function of FKBP proteins is to assist in protein folding and to act as molecular chaperones. They are also involved in the regulation of [[cell signaling]] pathways. FKBP12, one of the most studied members of this family, binds to the [[calcium]] release channel [[ryanodine receptor]] and modulates its activity.
-== See also ==
+== Clinical Significance ==
+FKBP proteins are significant in the field of [[immunology]] due to their role in the mechanism of action of immunosuppressive drugs like Tacrolimus. By binding to FKBP, Tacrolimus inhibits the activity of [[calcineurin]], a phosphatase involved in T-cell activation, thereby suppressing the immune response. This makes FKBP proteins a target for therapeutic interventions in [[organ transplantation]] and [[autoimmune diseases]].
+== Related pages ==
 * [[Immunophilin]]
+* [[Tacrolimus]]
 * [[Protein folding]]
-* [[Signal transduction]]
+* [[Molecular chaperone]]
-* [[Apoptosis]]
-* [[Osteogenesis imperfecta]]
-== References ==
-{{reflist}}
 [[Category:Proteins]]
 [[Category:Immunology]]
-[[Category:Cell biology]]
-{{protein-stub}}