title: Crystallization and preliminary X-ray crystallographic analysis of the human kindlin-2 PH domain.
abstract: 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).
authors.affiliation: Korea Polar Research Institute, Incheon, Republic of Korea. junhyucklee@kopri.re.kr
authors.forename: Jun Hyuck
authors.initials: JH
authors.lastname: Lee
authors.forename: Jun Yop
authors.initials: JY
authors.lastname: An
authors.forename: Hajeung
authors.initials: H
authors.lastname: Park
authors.forename: Hak Jun
authors.initials: HJ
authors.lastname: Kim
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry*; D016415:Sequence Alignment
chemical_list: C477322:FERMT3 protein, human; D008565:Membrane Proteins; D009363:Neoplasm Proteins