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Title
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Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1.
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Authors
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Y.Takai,
K.Kitano,
S.Terawaki,
R.Maesaki,
T.Hakoshima.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
49-51.
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PubMed id
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Abstract
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Radixin is a member of the ERM proteins that cross-link plasma membranes and
actin filaments. The FERM domains located in the N-terminal regions of ERM
proteins are responsible for membrane association through direct interaction
with the cytoplasmic tails of integral membrane proteins. Here, crystals of the
radixin FERM domain bound to the cytoplasmic peptides of two adhesion molecules,
CD43 and PSGL-1, have been obtained. Crystals of the radixin FERM domain bound
to CD43 belong to space group P4(3)22, with unit-cell parameters a = b = 68.72,
c = 201.39 A, and contain one complex in the crystallographic asymmetric unit.
Crystals of the radixin FERM domain bound to PSGL-1 belong to space group
P2(1)2(1)2(1), with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 A, and
contain two complexes in the crystallographic asymmetric unit. Intensity data
sets were collected to a resolution of 2.9 A for the FERM-CD43 complex and 2.8 A
for the FERM-PSGL-1 complex.
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