Sandbox Reserved 777: Difference between revisions
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== Introduction == | == Introduction == | ||
<Structure load='2H24' size='300' frame='true' align='right' caption='The interleukin 10 monomer' scene='Insert optional scene name here' /> | <Structure load='2H24' size='300' frame='true' align='right' caption='The interleukin 10 monomer. PDB 2H24' scene='Insert optional scene name here' /> | ||
Interleukin 10 (IL-10) belongs to a class of proteins called cytokines. Cytokines are chemical messengers that are produced by and act on cells of the immune system.'''(1)''' It is also part of the IL-10 family of cytokines, which also includes IL-19, IL-20, IL-22, IL-24 and IL-26. This grouping was made based on similarities in structure, function, and location of the encoding genes.'''(2)''' IL-10 has also previously been called cytokine synthesis inhibitory factor (CSIF) because of its anti-inflammatory properties and ability to inhibit the production of other cytokines.'''(3)''' The ability to limit the immune response to pathogens is crucial to preventing self-inflicted damage to the host. This cytokine is expressed in many eukaryotic hosts, as well as some viruses. A quick protein BLAST of the human IL-10 sequence reveals homology with IL-10 of many other primate species, as well as that found in bats, horses, elephants, rodents, sheep, cats and birds. The remainder of this page will focus on human IL-10. | Interleukin 10 (IL-10) belongs to a class of proteins called cytokines. Cytokines are chemical messengers that are produced by and act on cells of the immune system.'''(1)''' It is also part of the IL-10 family of cytokines, which also includes IL-19, IL-20, IL-22, IL-24 and IL-26. This grouping was made based on similarities in structure, function, and location of the encoding genes.'''(2)''' IL-10 has also previously been called cytokine synthesis inhibitory factor (CSIF) because of its anti-inflammatory properties and ability to inhibit the production of other cytokines.'''(3)''' The ability to limit the immune response to pathogens is crucial to preventing self-inflicted damage to the host. This cytokine is expressed in many eukaryotic hosts, as well as some viruses. A quick protein BLAST of the human IL-10 sequence reveals homology with IL-10 of many other primate species, as well as that found in bats, horses, elephants, rodents, sheep, cats and birds. The remainder of this page will focus on human IL-10. | ||
== Structure == | == Structure == | ||
[[Image:4helixbundle.png|300px|left|thumb|The four-helix bundle]] | [[Image:4helixbundle.png|300px|left|thumb|The four-helix bundle]] | ||
The cytokine structure is an intercalated dimer of two identical polypeptide chains, each 178 amino acids in length.'''(4)''' The monomers are made up of six amphipathic helices, with two helices of one monomer interacting with four of the other monomer, creating two distinct domains.A four-helix bundle is made up of helices A, C, D and F’ (and A’, C’ D’ and F). This feature is a signature element of all helical cytokines.'''(5)''' The structure is stabilized by <scene name='56/564053/Il-10_disulfide_bonds/2'>two disulfide bridges</scene> formed between the first and third cysteine residues and the second and fourth cysteine residues (Cys12 with Cys108, and Cys62 with Cys114). In the image, the disulfide bridges are shown in yellow. Reduction of the disulfide bonds in recombinant IL-10 has been shown to reduce helical content measured by circular dichroism and results in a lack of in vitro biological activity.'''(6)''' | The cytokine structure is an intercalated dimer of two identical polypeptide chains, each 178 amino acids in length.'''(4)''' The monomers are made up of six amphipathic helices, with two helices of one monomer interacting with four of the other monomer, creating two distinct domains.A four-helix bundle is made up of helices A, C, D and F’ (and A’, C’ D’ and F). This feature is a signature element of all helical cytokines.'''(5)''' The structure is stabilized by <scene name='56/564053/Il-10_disulfide_bonds/2'>two disulfide bridges</scene> formed between the first and third cysteine residues and the second and fourth cysteine residues (Cys12 with Cys108, and Cys62 with Cys114). In the image, the disulfide bridges are shown in yellow. Reduction of the disulfide bonds in recombinant IL-10 has been shown to reduce helical content measured by circular dichroism and results in a lack of in vitro biological activity.'''(6)'''[[Image:1ilk bio r 500.jpg |right|thumb| another view of the biologically active homodimer]] | ||
== Protein Expression == | == Protein Expression == | ||
