 |
PDBsum entry 2d2q
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
2d2q
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of dimerized radixin ferm domain suggests a novel masking motif in c-Terminal residues 295-304.
|
|
|
Authors
|
|
K.Kitano,
F.Yusa,
T.Hakoshima.
|
|
|
Ref.
|
|
Acta Crystallograph Sect F Struct Biol Cryst Commun, 2006,
62,
340-345.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion
molecules in the formation of the membrane-associated cytoskeleton. The binding
site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the
inactive form. A conventional masking motif, strand 1 (residues 494-500 in
radixin), has previously been identified in the C-terminal tail domain. Here,
the crystal structure of dimerized radixin FERM domains (residues 1-310) is
presented in which the binding site of one molecule is occupied by the
C-terminal residues (residues 295-304, strand 2) of the other molecule. The
residues contain a conserved motif that is compatible with that identified in
the adhesion molecules. The residues might serve as a second masking region in
the inactive form of ERM proteins.
|
|
|
|
|
|
Figure 1.
Figure 1 Crystal structure of dimerized radixin FERM domains.
(a) Overall structure as a ribbon model. Mol-1 is shown in light
blue and Mol-2 in pink, with its C-terminal extended residues
(Arg295-Gln304) in red. The radixin FERM domain consists of
subdomains A (the N-terminal 82 residues), B (residues 96-119)
and C (residues 204-297). (b) A side view shows that Mol-1 and
Mol-2 are aligned in a similar orientation. The blue dashed line
represents the membrane-interaction surface of a dimer and blue
arrows indicate binding sites to phosphatidylinositol
4,5-bisphosphate (PIP2; Hamada, Shimizu et al., 2000[Hamada, K.,
Shimizu, T., Matsui, T., Tsukita, S. & Hakoshima, T. (2000).
EMBO J. 19, 4449-4462.]). Figures were prepared using PyMOL
(http://pymol.sourceforge.net ). (c) Schematic representation of
the interactions between the C-terminal extended residues
(strand 2 in pink) and subdomain C (light blue). Hydrogen bonds
are shown as dashed lines and distances are indicated.
|
|
|
|
|
|
The above figure is
reprinted
from an Open Access publication published by the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2006,
62,
340-345)
copyright 2006.
|
|
|
|
|
|
|
