 |
PDBsum entry 1u35
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein/DNA
|
PDB id
|
|
|
|
1u35
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
98 a.a.
|
|
|
|
|
|
|
|
|
|
|
79 a.a.
|
|
|
|
|
|
|
|
|
|
|
106 a.a.
|
|
|
|
|
|
|
|
|
|
|
93 a.a.
|
|
|
|
|
|
|
|
|
|
|
83 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural characterization of the histone variant macroh2a.
|
|
|
Authors
|
|
S.Chakravarthy,
S.K.Gundimella,
C.Caron,
P.Y.Perche,
J.R.Pehrson,
S.Khochbin,
K.Luger.
|
|
|
Ref.
|
|
Mol Cell Biol, 2005,
25,
7616-7624.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
macroH2A is an H2A variant with a highly unusual structural organization. It has
a C-terminal domain connected to the N-terminal histone domain by a linker.
Crystallographic and biochemical studies show that changes in the L1 loop in the
histone fold region of macroH2A impact the structure and potentially the
function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region
reveals an alpha/beta fold which has previously been found in a functionally
diverse group of proteins. This region associates with histone deacetylases and
affects the acetylation status of nucleosomes containing macroH2A. Thus, the
unusual domain structure of macroH2A integrates independent functions that are
instrumental in establishing a structurally and functionally unique chromatin
domain.
|
|
|
|
|
|
|
