TBX3: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
| (2 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
=Introduction= | =Introduction= | ||
TBX3 acts as a repressor and has had its crystal structure solved to 1.7 Å resolution. There are many differences between the solved structure of TBX3 and its homologue, [[Brachyury]]. Secondary structures and quaternary contacts are slightly different. TBX3 independently recognises two halves of a palindromic site whereas Brachyury is stabilised via interactions between the two monomers. Despite this, the T-box domain of TBX3 and the T-box domain of Brachyury can be superimposed with a rmsd of 1.3 Å for 167 atoms. See [[Transcription and RNA Processing]]. | '''TBX3''' acts as a repressor and has had its crystal structure solved to 1.7 Å resolution. There are many differences between the solved structure of TBX3 and its homologue, [[Brachyury]]. Secondary structures and quaternary contacts are slightly different. TBX3 independently recognises two halves of a palindromic site whereas Brachyury is stabilised via interactions between the two monomers. Despite this, the T-box domain of TBX3 and the T-box domain of Brachyury can be superimposed with a rmsd of 1.3 Å for 167 atoms. See [[Transcription and RNA Processing]]. | ||
=Crystal structure= | =Crystal structure= | ||
{{STRUCTURE_1h6f| PDB=1h6f | SIZE=400| SCENE= |right|CAPTION=TBX3 complex with DNA and Mg+2 ion, [[1h6f]] }} | {{STRUCTURE_1h6f| PDB=1h6f | SIZE=400| SCENE= |right|CAPTION=TBX3 dimer complex with DNA and Mg+2 ion, [[1h6f]] }} | ||
TBX3 expressed from residues 101 - 291 were viable proteins and were crystallised in space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>. These included two monomers and one DNA duplex in the asymmetric unit. The monomers themselves can be superimposed to give an rmsd of 0.5 Å. The largest differences between the TBX3 crystal structure and the T-box domain of Brachyury is between residues 173 and 184, and between strands F and G. Four residues are inserted between F and G and this adopts a 3<sub>10</sub> conformation. | TBX3 expressed from residues 101 - 291 were viable proteins and were crystallised in space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>. These included two monomers and one DNA duplex in the asymmetric unit. The monomers themselves can be superimposed to give an rmsd of 0.5 Å. The largest differences between the TBX3 crystal structure and the T-box domain of Brachyury is between residues 173 and 184, and between strands F and G. Four residues are inserted between F and G and this adopts a 3<sub>10</sub> conformation. | ||
| Line 25: | Line 25: | ||
=3D structures of TBX3= | =3D structures of TBX3= | ||
[[ | [[T-box proteins]] | ||
=Additional Resources= | =Additional Resources= | ||
For additional information, see: [[Transcription and RNA Processing]] | For additional information, see: [[Transcription and RNA Processing]] | ||
<br /> | <br /> | ||
==Reference== | |||
<ref group="xtra">PMID:12005433</ref><references group="xtra"/> | |||
[[Category: Homo sapiens]] | |||
[[Category: Coll, M.]] | |||
[[Category: Muller, C W.]] | |||
[[Category: Developmental protein]] | |||
[[Category: Dna-binding]] | |||
[[Category: Holt-oram-syndrome]] | |||
[[Category: Ig-fold]] | |||
[[Category: Nuclear protein]] | |||
[[Category: Repressor]] | |||
[[Category: T-box transcription factor]] | |||
[[Category: Tbx3]] | |||
[[Category: Ulnar-mammary syndrome]] | |||