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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.

Original publication

DOI

10.1074/jbc.M112.365932

Type

Journal article

Journal

Journal of Biological Chemistry

Publication Date

26/10/2012

Volume

287

Pages

36990 - 36998