Sandbox Reserved 1647: Difference between revisions

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The secondary structure of the protein allows it to bind with the DNA : The T-box domain consists of several repeats of β-strands and α-helices and is involved in both dimerization and DNA binding. The crystal structure of the α-helices of the T-box domain bound to DNA strongly suggests that the amino group of <scene name='86/868180/Lys314/1'>K 313</scene> is associated with the phosphate of a DNA base via hydrogen-bond interaction.

Thanks to some post-translational modifications of the protein’s residues, the transcription factor TBX21 can bind with DNA and some proteins. Firstly, the ubiquitination of the residue <scene name='86/868180/Lys314/1'>K 313</scene> allows TBX21 to bind with the DNA sequence. Secondly, the phosphorylation of some residues allows TBX21 to interact with several proteins : the phosphorylation of <scene name='86/868180/Thr302/1'>T 302</scene> allows TBX21 to interact with NFAT, the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with RUNX1, the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with NF-кB p65 and finaly the one of Y525 allows the interaction with GATA-3.

Thanks to some post-translational modifications of the protein’s residues, the transcription factor TBX21 can bind with DNA and some proteins. Firstly, the ubiquitination of the residue <scene name='86/868180/Lys314/1'>K 313</scene> allows TBX21 to bind with the DNA sequence.Lys-313 was lately found as a key site required for T-bet to interact with the IFN-γ gene promoter and to assure phosphorylation at Thr-302. Secondly, the phosphorylation of some residues allows TBX21 to interact with several proteins : the phosphorylation of <scene name='86/868180/Thr302/1'>T 302</scene> allows TBX21 to interact with NFAT, the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with RUNX1, the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with NF-кB p65 and finaly the one of Y525 allows the interaction with GATA-3.

Sandbox Reserved 1647: Difference between revisions

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Revision as of 18:22, 14 January 2021 view source Thomas Dreo (talk \| contribs) 16 edits No edit summary ← Older edit		Revision as of 18:32, 14 January 2021 view source Justine Marc (talk \| contribs) 11 edits No edit summary Newer edit →
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	The secondary structure of the protein allows it to bind with the DNA : The T-box domain consists of several repeats of β-strands and α-helices and is involved in both dimerization and DNA binding. The crystal structure of the α-helices of the T-box domain bound to DNA strongly suggests that the amino group of <scene name='86/868180/Lys314/1'>K 313</scene> is associated with the phosphate of a DNA base via hydrogen-bond interaction.		The secondary structure of the protein allows it to bind with the DNA : The T-box domain consists of several repeats of β-strands and α-helices and is involved in both dimerization and DNA binding. The crystal structure of the α-helices of the T-box domain bound to DNA strongly suggests that the amino group of <scene name='86/868180/Lys314/1'>K 313</scene> is associated with the phosphate of a DNA base via hydrogen-bond interaction.
	Thanks to some post-translational modifications of the protein’s residues, the transcription factor TBX21 can bind with DNA and some proteins. Firstly, the ubiquitination of the residue <scene name='86/868180/Lys314/1'>K 313</scene> allows TBX21 to bind with the DNA sequence. Secondly, the phosphorylation of some residues allows TBX21 to interact with several proteins : the phosphorylation of <scene name='86/868180/Thr302/1'>T 302</scene> allows TBX21 to interact with NFAT, the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with RUNX1, the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with NF-кB p65 and finaly the one of Y525 allows the interaction with GATA-3.		Thanks to some post-translational modifications of the protein’s residues, the transcription factor TBX21 can bind with DNA and some proteins. Firstly, the ubiquitination of the residue <scene name='86/868180/Lys314/1'>K 313</scene> allows TBX21 to bind with the DNA sequence.Lys-313 was lately found as a key site required for T-bet to interact with the IFN-γ gene promoter and to assure phosphorylation at Thr-302. Secondly, the phosphorylation of some residues allows TBX21 to interact with several proteins : the phosphorylation of <scene name='86/868180/Thr302/1'>T 302</scene> allows TBX21 to interact with NFAT, the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with RUNX1, the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with NF-кB p65 and finaly the one of Y525 allows the interaction with GATA-3.