 |
|
Title
|
|
Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF).
|
|
|
Authors
|
|
S.Terawaki,
R.Maesaki,
K.Okada,
T.Hakoshima.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2003,
59,
177-179.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Radixin is a member of the ERM proteins, which cross-link plasma membranes and
actin filaments. The N-terminal FERM domains of ERM proteins interact with
Na(+)/H(+)-exchanger regulatory factors (NHERFs), which are PDZ-containing
adaptor proteins, to modulate the ion-channel activity. Here, crystals of
complexes between the radixin FERM domain and the C-terminal regions of NHERF
and NHERF2 have been obtained. The crystals of the FERM-NHERF complex were found
to belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 69.38 (2),
b = 146.27 (4), c = 177.76 (7) A. The crystal contains four complexes in the
asymmetric unit. An intensity data set was collected to a resolution of 2.50 A.
|
|
|
|