This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Anti-silencing factor

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
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.
 +
 +
==3D structures of anti-silencing factor==
 +
[[Anti-silencing factor 3D structures]]
</StructureSection>
</StructureSection>

Revision as of 08:07, 18 March 2019

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

Drag the structure with the mouse to rotate

3D structures of anti-silencing factor

Updated on 18-March-2019

1roc, 1wg3 – yASF – yeast
2idc – yASF/H3
1tey – hASF N terminal – human - NMR
2io5 – hASF + histone H3.1 + histone H4
2hue - yASF + histone H3 + histone H4
4eo5 - yASF + histone H3.2 (mutant) + histone H4 (mutant)
2z3f – yASF + SPCIA1
2i32 – hASF + HIRA
2z34 – hASF N terminal + HIR1
3aad – hASF + transcription initiation factor TFIID
2ygv – yASF + serine/threonine protein kinase RAD53

References

  1. Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R. Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972 doi:10.1038/nsmb1147

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools