Sandbox Reserved 1647
From Proteopedia
Line 2: | Line 2: | ||
<Structure load='5t1j' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='5t1j' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
==Introduction== | ==Introduction== | ||
- | TBX21 or T-bet is a [https://en.wikipedia.org/wiki/Transcription_factor transcription factor], more precisely a [[T-box proteins]]. T-bet has a dimer structure composes of two identical chains (A / B ) with a total molecular weight of 76,37 kDA. Its binding domain allows it to bind itself to the DNA on promotor or regulator area. The particularity of this T-box protein is that is able to link two DNA molecules or two areas of the same DNA molecules which are far from each other. | + | TBX21 or T-bet is a [https://en.wikipedia.org/wiki/Transcription_factor transcription factor], more precisely a [[T-box proteins]]. T-bet has a dimer structure composes of two identical chains (A / <scene name='86/868180/Chain_b/1'>B</scene> ) with a total molecular weight of 76,37 kDA. Its binding domain allows it to bind itself to the DNA on promotor or regulator area. The particularity of this T-box protein is that is able to link two DNA molecules or two areas of the same DNA molecules which are far from each other. |
== Structure and structural interactions == | == Structure and structural interactions == |
Revision as of 12:23, 14 January 2021
This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664. |
To get started:
More help: Help:Editing |
|
Contents |
Introduction
TBX21 or T-bet is a transcription factor, more precisely a T-box proteins. T-bet has a dimer structure composes of two identical chains (A / ) with a total molecular weight of 76,37 kDA. Its binding domain allows it to bind itself to the DNA on promotor or regulator area. The particularity of this T-box protein is that is able to link two DNA molecules or two areas of the same DNA molecules which are far from each other.
Structure and structural interactions
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
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 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 K313 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 K313 allows TBX21 to bind with the DNA sequence. Secondly, the phosphorylation of some residues allows TBX21 to interact with several proteins : the phosphorylation of T302 allows TBX21 to interact with NFAT, the one of Y304 allows TBX21 to interact with RUNX1, the one of S508 allows the interaction with NF-кB p65 and finally the one of Y525 allows the interaction with GATA-3.
Functions
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644