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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 ?-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).

SUBMITTER: Lee JH

PROVIDER: S-EPMC3107146 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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

Lee Jun Hyuck JH An Jun Yop JY Park Hajeung H Kim Hak Jun HJ Eom Soo Hyun SH

Acta crystallographica. Section F, Structural biology and crystallization communications 20110526 Pt 6

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 prot ...[more]

PMID: 21636915

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