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Journal article

Structure of three tandem filamin domains reveals auto-inhibition of ligand binding

Abstract:

Human filamins are large actin-crosslinking proteins composed of an N-terminal actin-binding domain followed by 24 Ig-like domains (IfFLNs), which interact with numerous transmembrane receptors and cytosolic signaling proteins. Here we report the 2.5 Å resolution structure of a three-domain fragment of human filamin A (IgFLNa19-21). The structure reveals an unexpected domain arrangemetn, with IgFLNa20 partially unfolded bringing IgFLNa21 into close proximity to IgFLNa19. Notably the N-terminu...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/sj.emboj.7601827

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Institution:
"Yale University School of Medicine, USA"
Department:
Department of Pharmacology and Interdepartmental Program in Vascular Biology and Transplantation
Role:
Author
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Institution:
"University of Oulu, Finland"
Department:
Department of Biochemistry and Biocenter Oulu
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Institution:
"University of Jyväskylä, Finland"
Department:
Department of Biological and Environmental Science
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Contributors

Institution:
University of Oxford
Role:
Other
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Funding agency for:
Calderwood, D
Grant:
ROI GM068600-01
CSC - the Finnish IT Centre for Science More from this funder
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Funding agency for:
Ylänne, J
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Funding agency for:
Jiang, P
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Funding agency for:
Coles, C
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Publisher:
Nature Publishing Group Publisher's website
Journal:
EMBO Journal Journal website
Volume:
26
Issue:
17
Pages:
3993-4004
Publication date:
2007-09-01
DOI:
ISSN:
1460-2075
Language:
English
Keywords:
Subjects:
UUID:
uuid:593888b0-7bdb-4588-a3df-8acc77db2121
Local pid:
ora:3162
Deposit date:
2009-12-15

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