Open AccessCrystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane‐type 1 matrix metalloproteinase (MT1‐MMP)
Author(s) -
Terawaki Shinichi,
Kitano Ken,
Aoyama Miki,
Hakoshima Toshio
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108026869
Subject(s) - radixin , cytoplasm , membrane , extracellular matrix , ferm domain , matrix metalloproteinase , biophysics , cell membrane , chemistry , crystallography , membrane protein , microbiology and biotechnology , integral membrane protein , cytoskeleton , biology , cell , biochemistry , ezrin
ERM proteins play a role in the cross‐linking found between plasma membranes and actin filaments. The N‐terminal FERM domains of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. During cell migration and movement, membrane‐type 1 matrix metalloproteinase (MT1‐MMP) on plasma membranes sheds adhesion molecule CD44 in addition to degrading the extracellular matrix. Here, the interaction between the radixin FERM domain and the MT1‐MMP cytoplasmic tail is reported and preliminary crystallographic characterization of crystals of the radixin FERM domain bound to the cytoplasmic tail of MT1‐MMP is presented. The crystals belong to space group P 6 1 22, with unit‐cell parameters a = b = 122.7, c = 128.3 Å, and contain one complex in the crystallographic asymmetric unit. The diffraction data were collected to a resolution of 2.4 Å.