Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the human kindlin‐2 PH domain
Author(s) -
Lee Jun Hyuck,
An Jun Yop,
Park HaJeung,
Kim Hak Jun,
Eom Soo Hyun
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111013820
Subject(s) - pleckstrin homology domain , ferm domain , integrin , focal adhesion , crystallization , crystallography , cytoskeleton , cytoplasm , biophysics , chemistry , microbiology and biotechnology , biology , membrane protein , membrane , biochemistry , integral membrane protein , receptor , signal transduction , organic chemistry , cell
Kindlins contribute to the correct assembly of integrin‐containing focal adhesion sites through their direct interaction with the cytoplasmic tail of β‐integrin. The FERM domain of kindlins has a unique subdomain organization: the F2 subdomain harbours a centrally located pleckstrin homology (PH) domain that is thought to be involved in the membrane targeting of kindlins. FERM domains are found in a number of cytoskeletal proteins that mediate the interaction between integrins and cytosolic proteins. In the present study, the PH domain of human kindlin‐2 was subcloned, solubly expressed in Escherichia coli and crystallized using the hanging‐drop vapour‐diffusion method. A diffraction data set was collected at 2.8 Å resolution using synchrotron radiation on BL‐4A at the Pohang Accelerator Laboratory (Pohang, Republic of Korea).