Journal article icon

Journal article

Structure of the bone morphogenetic protein receptor ALK2 and implications for fibrodysplasia ossificans progressiva

Abstract:
Background: Mutations in the ALK2 kinase cause extraskeletal bone formation. Results: We solved the structure of ALK2 in complex with the inhibitor FKBP12. Conclusion: Disease mutations break critical interactions that stabilize the inactive ALK2-FKBP12 complex leading to kinase activation. Significance: We offer an explanation for the effects of mutation and a structural template for the design of small molecule inhibitors. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More from this funder
Name:
University of Oxford
Funding agency for:
Sanvitale, C
Grant:
FOP Research Fund
More from this funder
Name:
Roemex
Funding agency for:
Kerr, G
Journal:
Journal of Biological Chemistry More from this journal
Volume:
287
Issue:
44
Pages:
36990-36998
Publication date:
2012-10-26
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:359721
UUID:
uuid:f3baf9ad-c9dd-4e8a-abcc-df9bce12be05
Local pid:
pubs:359721
Source identifiers:
359721
Deposit date:
2013-11-16

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP