Crystallization and preliminary X-ray crystallographic analysis of the human Kindlin-2 PH domain

Abstract

Kindlins contribute the correct assembly of integrin-containing focal adhesion sites through their direct interaction with the cytoplasmic tail of β-integrins. The FERM domain of kindlins has a unique subdomain organization: the F2 subdomain harbors a centrally located pleckstrin homology (PH) domain 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 vapor-diffusion method. A diffraction data set was collected at 2.8 ？resolution using a synchrotron X-ray radiation source at the BL- 4A of the Pohang Accelerator Laboratory (Pohang, Korea).domain harbors a centrally located pleckstrin homology (PH) domain 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 vapor-diffusion method. A diffraction data set was collected at 2.8 ？resolution using a synchrotron X-ray radiation source at the BL- 4A of the Pohang Accelerator Laboratory (Pohang, Korea).