Sandbox Reserved 1647: Difference between revisions

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=== Secondary structure and interactions ===
=== Secondary structure and interactions ===


The secondary structure of the protein allows it to bind with the DNA : the T-box domain consists of several repeats of <scene name='86/868180/Helix_and_strand/1'>β-strands and α-helix</scene> and is involved in both dimerization and DNA binding.
The secondary structure of the protein allows it to bind to the DNA : the T-box domain consists of multiple <scene name='86/868180/Helix_and_strand/1'>β-strands and α-helix</scene> repeats and is involved in both dimerization and DNA binding.
Thanks to some [https://en.wikipedia.org/wiki/Post-translational_modification post-translational modifications] of the protein’s residues, the transcription factor TBX21 can bind with DNA between the residues <scene name='86/868180/Lys135/2'>LYS 135</scene> and <scene name='86/868180/Asn_326/4'>ASN 326</scene> and some proteins. Firstly, ubiquitination of K 313 residue allows TBX21 to bind to the DNA sequence. Lys-313 was recently found to be a key site required for the interaction of T-bet with the [https://proteopedia.org/wiki/index.php/6f1e IFN-γ] gene promoter and the phosphorylation at Thr-302 <ref name="Lysine 313 of T-box is crucial for modulation of protein stability, DNA binding, and threonine phosphorylation of T-bet">DOI 10.1073/pnas.0409512102</ref>. Secondly, phosphorylation of some residues allows TBX21 to interact with several proteins. For example, phosphorylation of T 302 allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of Y 304 with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], that of S 508 with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally the one of Y525 allows the interaction with <scene name='86/868180/Dna_binding_by_gata_transcript/2'>GATA-3</scene> <ref name="The transcription factors T-bet and GATA-3 control alternative pathways of T-cell differentiation through a shared set of target genes">DOI 10.1073/pnas.0909357106</ref>.
Thanks to some [https://en.wikipedia.org/wiki/Post-translational_modification post-translational modifications] of the protein’s residues, the transcription factor TBX21 can bind with DNA between the residues <scene name='86/868180/Lys135/2'>LYS 135</scene> and <scene name='86/868180/Asn_326/4'>ASN 326</scene> and some proteins. Firstly, ubiquitination of K 313 residue allows TBX21 to bind to the DNA sequence. Lys-313 was recently found to be a key site required for the interaction of T-bet with the [https://proteopedia.org/wiki/index.php/6f1e IFN-γ] gene promoter and the phosphorylation at Thr-302 <ref name="Lysine 313 of T-box is crucial for modulation of protein stability, DNA binding, and threonine phosphorylation of T-bet">DOI 10.1073/pnas.0409512102</ref>. Secondly, phosphorylation of some residues allows TBX21 to interact with several proteins. For example, phosphorylation of T 302 allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of Y 304 with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], that of S 508 with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally the one of Y525 allows the interaction with <scene name='86/868180/Dna_binding_by_gata_transcript/2'>GATA-3</scene> <ref name="The transcription factors T-bet and GATA-3 control alternative pathways of T-cell differentiation through a shared set of target genes">DOI 10.1073/pnas.0909357106</ref>.


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