Anti-silencing factor: Difference between revisions

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ASF has an 80 residue segment which binds RNA at the N-terminal and a C-terminal which is composed of 80% Ser and Arg.
ASF has an 80 residue segment which binds RNA at the N-terminal and a C-terminal which is composed of 80% Ser and Arg.
</StructureSection>


==3D structures of anti-silencing factor==
==3D structures of anti-silencing factor==
[[Anti-silencing factor 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
 
[[1roc]], [[1wg3]] – yASF – yeast<br />
[[2idc]] – yASF/H3<br />
[[1tey]] – hASF N terminal – human - NMR<br />
[[2io5]] – hASF + histone H3.1 + histone H4<br />
[[2hue]] - yASF + histone H3 + histone H4<br />
[[4eo5]] - yASF + histone H3.2 (mutant) + histone H4 (mutant) <br />
[[2z3f]] – yASF + SPCIA1<br />
[[2i32]] – hASF + HIRA<br />
[[2z34]] – hASF N terminal + HIR1<br />
[[3aad]] – hASF + transcription initiation factor TFIID<br />
[[2ygv]] – yASF + serine/threonine protein kinase RAD53


==References==
==References==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 08:08, 18 March 2019

Structure of yeast anti-silencing factor complex with Br- ions (PDB entry 1roc)

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References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky