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. 2008 Nov 21;283(47):32831–32838. doi: 10.1074/jbc.M801266200

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Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 7. — Structural differences between activin A and BMP may explain antagonist specificity. a and b, superposition of BMP2 and BMP7 onto the FSTL3·activin A complex, aligning only monomer 1 of activin A. The ribbon of activin A is shown, but for clarity, only the prehelix loop residues for each BMP (BMP2 (pink) and BMP7 (purple)) are depicted. The dotted lines indicate regions on BMP close enough to clash with the N-terminal domains. These appear more extensive for FSTL3. c, overall scheme for FSTL3 and FS binding to activin A and BMPs. We propose that the N-terminal domain of FS-type antagonists does not interact favorably with BMPs, thus accounting for the decreased affinity. We propose that the low affinity still observed for FS may be a result of the FS(ND)FS(FSD3) interactions and/or structural variation in the antagonist N-terminal domains.

Inline graphic — Structural differences between activin A and BMP may explain antagonist specificity. a and b, superposition of BMP2 and BMP7 onto the FSTL3·activin A complex, aligning only monomer 1 of activin A. The ribbon of activin A is shown, but for clarity, only the prehelix loop residues for each BMP (BMP2 (pink) and BMP7 (purple)) are depicted. The dotted lines indicate regions on BMP close enough to clash with the N-terminal domains. These appear more extensive for FSTL3. c, overall scheme for FSTL3 and FS binding to activin A and BMPs. We propose that the N-terminal domain of FS-type antagonists does not interact favorably with BMPs, thus accounting for the decreased affinity. We propose that the low affinity still observed for FS may be a result of the FS(ND)FS(FSD3) interactions and/or structural variation in the antagonist N-terminal domains.