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Journal article

Biophysical analysis of Kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif.

Abstract:

Kindlin-3, a 75-kDa protein, has been shown to be critical for hemostasis, immunity, and bone metabolism via its role in integrin activation. The Kindlin family is hallmarked by a FERM domain comprised of F1, F2, and F3 subdomains together with an N-terminal F0 domain and a pleckstrin homology domain inserted in the F2 domain. Recombinant Kindlin-3 was cloned, expressed, and purified, and its domain organization was studied by x-ray scattering and other techniques to reveal an extended confor...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m112.415208

Authors


Füzéry, AK More by this author
Campbell, ID More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Journal:
The Journal of biological chemistry
Volume:
287
Issue:
45
Pages:
37715-37731
Publication date:
2012-11-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:264659f7-1b13-4ba9-aaa5-311b3515bc05
Source identifiers:
352416
Local pid:
pubs:352416

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