P73: Difference between revisions

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{{STRUCTURE_2xwc|  PDB=2xwc  | SIZE=400| SCENE= |right|CAPTION=Human p73 DNA-binding domain complex with Tris, glycerol and Zn+2 ion, [[2xwc]] }}
<StructureSection load='' size='350' side='right' caption='Human p73 DNA-binding domain complex with Tris, glycerol and Zn+2 ion (grey), [[2xwc]]' scene='46/468230/Cv/2' pspeed='8'>


'''p73''' is a protein related to p53 tumor supressor.  It is involved in cell cycle regulation and induction of apoptosis.  P73 has several vatiants differing in their C- or N-terminal.
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'''p73''' is a protein related to p53 tumor suppressor.  It is involved in cell cycle regulation and induction of apoptosis<ref>PMID:9891077</ref>.  p73 has several variants differing in their C- or N-terminal.  p73 contains DNA-binding domain (DBD residues 112-312); tetramerization domain (TD residues 351-398).
== Structural highlights ==
*<scene name='46/468230/Cv/5'>1st Zn coordination site</scene>.
*<scene name='46/468230/Cv/6'>2nd Zn coordination site</scene>.
</StructureSection>
== 3D Structures of p73 ==
== 3D Structures of p73 ==


[[1cok]] – hp73 C terminal – human – NMR
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


[[2kby]] – hp73 tetramerization domain – NMR
Domains - DNA-binding (DBD) 112-311; Tetramerization (TD) 351-398; C-terminal 439-506.


[[2wqi]], [[2wqj]], [[2wtt]] - hp73 tetramerization domain
[[1cok]] hp73 C terminal – human – NMR


[[2xwc]] – hp73 DNA-binding domain (mutant)
[[2kby]] – hp73 TD – NMR


[[2wqi]], [[2wqj]], [[2wtt]] - hp73 TD<br />
[[5hob]], [[5hoc]] - hp73 TD (mutant) <br />
[[2xwc]] – hp73 DBD (mutant)<br />
[[2nb1]] - hp73 TD (mutant) + hp63 TD (mutant)<br />
[[3vd0]], [[3vd1]], [[3vd2]], [[4g82]], [[4g83]], [[4guo]], [[4guq]], [[5kbd]], [[7ezj]] – hp73 DBD + DNA<br />
[[4a63]] – hp73 DBD + apoptosis stimulating of p53 protein<br />
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman