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

Cited 3 time in scopus
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Title
Crystallization and preliminary X-ray crystallographic analysis of the human Kindlin-2 PH domain
Other Titles
Kindlin-2 PH domain 단백질의 삼차구조분석을 위한 결정화 및 X-선 회절데이타 분석
Authors
HaJeung Park
Jun Yop An
Lee, Jun Hyuck
Soo Hyun Eom
Kim, Hak Jun
Subject
Biochemistry & Molecular Biology; Biophysics; Crystallography
Keywords
focal adhesion; kindlin; pleckstrin homology domain; talin
Issue Date
2011
Publisher
International Union of Crystallography
Citation
HaJeung Park, et al. 2011. "Crystallization and preliminary X-ray crystallographic analysis of the human Kindlin-2 PH domain". ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 67(6): 696-699.
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).
URI
http://repository.kopri.re.kr/handle/201206/5833
DOI
http://dx.doi.org/10.1107/S1744309111013820
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