Stepler sandbox STAT3: Difference between revisions
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== Regulation == | == Regulation == | ||
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref> | |||
== DNA-Protein Interactions == | == DNA-Protein Interactions == | ||
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein interacts with DNA</scene> by binding to the major groove of the DNA. | The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein interacts with DNA</scene> by binding to the major groove of the DNA. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/1'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
