Sandbox Reserved 1647: Difference between revisions

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=== 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 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 <scene name='86/868180/Helix_and_strand/1'>β-strands and α-helix</scene> and is involved in both dimerization and DNA binding.

~~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 [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally 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 between the residues <scene name='86/868180/Lys135/1'>LYS 135</scene> and <scene name='86/868180/Asn_326/1'>ASN 326</scene> 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 [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally the one of Y525 allows the interaction with GATA-3.

Sandbox Reserved 1647: Difference between revisions

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@@ Line 20: / Line 20: @@
 === 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 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 <scene name='86/868180/Helix_and_strand/1'>β-strands and α-helix</scene> and is involved in both dimerization and DNA binding.
-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 [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally 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 between the residues <scene name='86/868180/Lys135/1'>LYS 135</scene> and <scene name='86/868180/Asn_326/1'>ASN 326</scene> 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 [https://proteopedia.org/wiki/index.php/2o93 NFAT], the one of <scene name='86/868180/Tyr304/1'>Y 304</scene> allows TBX21 to interact with [https://proteopedia.org/wiki/index.php/1co1 RUNX1], the one of <scene name='86/868180/Ser508/1'>S 508</scene> allows the interaction with [https://proteopedia.org/wiki/index.php/2i9t NF-кB p65] and finally the one of Y525 allows the interaction with GATA-3.